Publications

2017

“How does your protein fold? Elucidating the Apomyoglobin Folding Pathways.” H.J. Dyson, and P.E. Wright (2017), Acc. Chem. Res. 50, 105-111.

“Hypersensitive termination of the hypoxic response by a disordered protein switch.” R.B. Berlow, H.J. Dyson, P.E. Wright (2017), Nature 543, 447-451.

“Role of the CBP catalytic core in intramolecular SUMOylation and control of histone H3 acetylation.” S. Park, R.L. Stanfield, M. A. Martinez-Yamout, H.J. Dyson, I.A. Wilson, P.E. Wright (2017), Proc. Natl. Acad. Sci., 114, E5335-E5342.

“Structural basis for interaction of the tandem zinc finger domains of human muscleblind with cognate RNA from human cardiac troponin T.” S. Park, P.D. Phukan, M. Zeeb, M.A. Martinez-Yamout, H.J. Dyson, P.E. Wright (2017), Biochemistry, 56, 4154-4168.

“Defining the structural basis for allosteric product release from E.coli dihydrofolate reductase using NMR relaxation dispersion.” D. Oyen, R. Fenwick, P. Aoto, R. Stanfield, I. Wilson, H.J. Dyson, P.E. Wright (2017), J. Amer. Chem. Soc., 139, 11233-11240.

“Marking the Milestones in Structural Biology.” P.E. Wright, H. Hodak (2017), J. Mol. Biol., 429, 2591-2593

2016

“Multi-probe Relaxation Dispersion Measurement Increase Sensitivity to Protein Dynamics.” R.Bryn Fenwick, D. Oyen, P.E. Wright (2016), Phys. Chem. Chem. Phys. 18, 5789-5798.

“Conformational Dynamics of a Membrane Protein Chaperone Enables Spatially-regulated Substrate Capture and Release.” F.C. Liang, G.J. Kroon, C. McAvoy, C. Chi, P. Wright, S. Shan (2016), Proc. Natl Acad. Sci 113, E1615-E1624.

“Role of Intrinsic Protein Disorder in the Function and Interactions of the Transcriptional Coactivators CBP and p300.” H.J. Dyson, P.E. Wright (2016), J. Biological Chemistry 291, 6714-6722.

“Recognition of the Disordered p53 Transactivation Domain by the Transcriptional Adapter Zinc Finder Domain of CREB-Binding Protein.” A.S. Krois, J.C. Ferreon, M.A. Martinez-Yamout, H.J. Dyson, P.E. Wright (2016), Proc. Natl Acad. Sci. 113, E1853-E1862.

“NMR Characterization of Information Flow and Allosteric Communities in the MAP Kinase p38γ.”  P.C. Aoto, B.T. Martin, P.E. Wright (2016) Sci. Rep. 6, 28655, DOI:10.1038/srep28655

Finding Our Way in the Dark Proteome.” A. Bhowmick, D. Brookes, S. Yost, H.J. Dyson, J. Forman-Kay, D. Gunter, M. Head-Gordon, G. Hura, V. Pande, D. Wemmer, P.E. Wright, T. Head-Gordon (2016) J. Amer. Chem.Soc., 138, 9730-9742.

“Solid-State NMR Studies Reveal Native-like Beta-sheet Structures in Transthyretin amyloid.” K.H. Lim, A.K.R. Dasari, I.F. Hung, Z. Gan, J.W. Kelly, P.E. Wright, D.E. Wemmer (2016) Biochemistry, 55, 5272-5278.

“Mapping the interactions of adenoviral E1A proteins with the p160 nuclear receptor coactivator binding domain of CBP.” P. Haberz, M. Arai, M.A. Martinez Yamout, H.J. Dyson, P.E. Wright (2016) Protein Science, 25, 2256-2267.

2015

Functional Advantages of Dynamic Protein Disorder.” R.B. Berlow, H. J. Dyson, P.E. Wright (2015), FEBS Letters, 589, 2433-2440.

Conformational propensities of intrinsically disordered proteins influence the mechanism of binding and folding.” M. Arai, K.Sugase, H.J. Dyson, P.E. Wright (2015), Proc. Natl Acad. Sci., 112, 9614-9619.

Cofactor-mediated conformational dynamics promote product release from E. coli dihydrofolate reductase via an allosteric pathway.” D. Oyen, R. Fenwick, R. Stanfield, H.J. Dyson, and P.E. Wright (2015), J. Amer. Chem. Soc., 137, 9459-9468.

Intrinsically Disordered Proteins in Cellular Signaling and Regulation.” P.E. Wright and H. J. Dyson (2015), Nature Rev. Mol. Cell Biol., 16, 18-29.

2014

Combinatorial Regulation of a Signal Dependent Activator by Phosphorylation and Acetylation.”  J.C. Paz, S. Park, N. Phillips, W. Liu, L. Kasper, P. Brindle, G. Zhang, M. Zhou, P.E. Wright and M. Montminy (2014), Proc. Natl Acad. Sci, 111, 17116-17121

“The High-Risk HPV16 E7 Oncoprotein Mediates Interaction Between the Transcriptional Coactivator CBP and the Retinoblastoma Protein pRb.” A.L. Jansma, M.A. Martinez-Yamout, R. Liao, P. Sun, H.J. Dyson and P.E. Wright (2014), J. Mol. Biol., 426, 4030-4048.

Assemblages: Functional units formed by cellular phase separation.” J. A., Toretsky and P.E. Wright (2014), J. Cell Biol., 206, 579-588

“Classification of Intrinsically Disordered Regions and Proteins.” R. van der Lee, M. Buljan, B. Lang, R.J. Weatheritt, G.W. Daughdrill, A.K. Dunker, M. Fuxreiter, J. Gough, J. Gsponer, D.T. Jones, P.M. Kim, R.W. Kriwacki, C.J. Oldfield, R.V. Pappu, P. Tompa, V.N. Uversky, P.E. Wright and M.M. Babu (2014), Chemical Reviews, 114, 6589-6631

“Accurate Scoring of Non-Uniform Sampling Schemes for Quantitative NMR.” P. Aoto, R.B. Fenwick, G.J.A. Kroon and P.E. Wright (2014), J. Mag. Res., 246, 31-35

“Probing the Non-Native H Helix Translocation in Apomyoglobin Folding Intermediates.” P. Aoto, C. Nishimura, H.J. Dyson and P.E. Wright (2014), Biochemistry, 53, 3767-3780

“Structural Characterization of Interactions between the Double-Stranded RNA-Binding Zinc Finger Protein JAZ and Nucleic Acids.”  R.G. Burge, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2014), Biochemistry, 53, 1495-1510

“Side Chain Conformational Averaging in Human Dihydrofolate Reductase.”  L.M. Tuttle, H.J. Dyson, P.E. Wright (2014), Biochemistry, 53, 1134-1145

“Integrated description of protein dynamics from room-temperature X-ray crystallography and NMR.”  R.B. Fenwick, H. van den Bedem, J.S. Fraser, P.E. Wright (2014), Proc. Natl Acad. Sci., 111, E445-E454

“pE-DB: a database of structural ensembles of intrinsically disordered and of unfolded proteins.” M. Varadi, S. Kosol, P. Lebrun, E. Valentini, M. Blackledge, A.K. Dunker, I.C. Felli, J.D. Forman-Kay, R.W. Kriwacki, R. Pieratelli, J. Sussman, D.I. Svergun, V.N. Uversky, M. Vendruscolo, D. Wishart, P.E. Wright, P. Tompa (2014), Nucleic Acids Research, 42, D326-D335

2013

“Mechanisms of Transthyretin Inhibition of β-Amyloid Aggregation In Vitro.” X. Li, X. Zhang, A.R. Ladiwala, D. Du, J.K. Yadav, P.M. Tessier, P.E. Wright, J.W. Kelly and J.N. Buxbaum (2013), Journal of Neuroscience, 33, 19423-19433

“Divergent evolution of protein conformational dynamics in dihydrofolate reductase.” G. Bhabha, D.C. Ekiert, M. Jennewein, C.M. Zmasek, L.M. Tuttle, G. Kroon, H.J. Dyson, A. Godzik, I.A. Wilson, and P.E. Wright (2013), Nature Struct. Mol. Biol., 20, 1243-1249

“Analysis of the RelA:CBP/p300 interaction reveals its involvement in NFkB-driven transcription.” S.P. Mukherjee, M. Behar, A. Hoffmann, P.E. Wright, and G. Ghosh (2013), PLOS Biology, 11, 1-20

“Automated identification of functional dynamic contact networks from X-ray crystallography.”  H. van den Bedem, G. Bhabha, K. Yang, P.E. Wright, and J.S. Fraser (2013), Nature Methods, 10, 896-902 (News & Views by M.A. Wilson in Nature Methods 10, 835-837, 2013; Research Highlight: Nature Struct. Mol. Biol. 20, 1025, 2013; Nature Chem. Biol. 9, 600, 2013)

“The CH2 domain of CBP/p300 is a novel zinc finger.”  S. Park, M.A. Martinez-Yamout, H.J. Dyson, P.E. Wright (2013), FEBS Letters, 587, 2506-2511

“A distal mutation perturbs dynamic amino acid networks in dihydrofolate reductase.”  D.D. Boehr, J.R. Schnell, D. McElheny, S.H. Bae, B.M. Duggan, S.J. Benkovic, H.J. Dyson, P.E. Wright (2013), Biochemistry, 52, 4605-4619

“Fast and accurate fitting of relaxation dispersion data using the flexible software package GLOVE.”  K. Sugase, T. Konuma, J.C. Lansing, P.E. Wright (2013), J. Biomolecular NMR, 56, 275-283

“Modulation of allostery by protein intrinsic disorder.” A.C.M. Ferreon, J.C. Ferreon,  P.E. Wright, and A.A. Deniz (2013), Nature, 498, 390-394 (News & Views by V.J. Hilser in Nature 498, 308-310, 2013; featured paper in Cell Leading Edge Select (August 2013), Chemical & Engineering News (Jun 2013); Faculty of 1000 Recommended Paper)

“Side-Chain Conformational Heterogeneity of Intermediates in the Escherichia coli Dihydrofolate Reductase Catalytic Cycle.”  L.M. Tuttle, H.J. Dyson, P.E. Wright (2013), Biochemistry, 52, 3464-3477

“Localized structural fluctuations promote amyloidogenic conformations in transthyretin.” K.H. Lim, H.J. Dyson, J.W. Kelly, and P.E. Wright (2013), Journal of Molecular Biology, 425, 977-988

2012

“Molecular basis for recognition of methylated and specific DNA sequences by the zinc finger protein Kaiso.” B.A. Buck-Koehntop, R.L. Stanfield, D.C. Ekiert, M.A. Martinez-Yamout, H.J. Dyson, I.A. Wilson and P.E. Wright (2012), Proc. Natl Acad. Sci., 109, 15229-15234

“Wright, Peter E.: From Inorganic Chemistry to Protein Structural Dynamics.”  P.E. Wright (2012)  InEncyclopedia of Magnetic Resonance, (R.K. Harris & R.E. Wasylishen, eds.), John Wiley & Sons, Ltd., Chichester DOI: 10.1002/9780470034590.emrhp1070.

“Quantitative analysis of multisite protein ligand interactions by NMR: binding of intrinsically disordered p53 transactivation subdomains with the TAZ2 domain of CBP.”  M. Arai, J.C. Ferreon, and P.E. Wright (2012), J. Amer. Chem. Soc., 134, 3792-3803

“Kaiso uses all Three Zinc Fingers and Adjacent Sequence Motifs for High Affinity Binding to Sequence-specific and Methyl-CpG DNA Targets.”  B. Buck-Koehntop, M. Martinez-Yamout, H.J. Dyson, P.E. Wright (2012), FEBS Letters, 586, 734-739

2011

“Identification of endogenous ligands bound to bacterially expressed human and E. coli dihydrofolate reductase by 2D NMR.”  G. Bhabha, L. Tuttle, M. Martinez-Yamout, P.E. Wright (2011), FEBS Letters, 585, 3528-3532

“Measurement of protein unfolding/refolding kinetics and structural characterization of hidden intermediates by NMR relaxation dispersion” D.W. Meinhold, P.E. Wright (2011), Proc. Natl Acad. Sci., 108(22) (9078-83)

“Consequences of Stabilizing the Natively Disordered F helix for the Folding Pathway of Apomyoglobin” C. Nishimura, H.J. Dyson, P.E. Wright (2011), J. Mol. Biol, 411, 248-263

“A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis”G. Bhabha, J. Lee, D.C. Ekiert, J. Gam, I.A. Wilson, H. J. Dyson and P.E. Wright (2011), Science, 332 (234-238)

2010

“Leu628 of the KIX Domain of CBP is a Key Residue for the Interaction with the MLL Transactivation Domain” M. Arai, H.J. Dyson and P.E. Wright (2010), FEBS Letters, 584, 4500-4504

 “Graded Enhancement of p53 binding to CREB-binding protein (CBP) by multisite phosphorylation” C.W. Lee, J.C. Ferreon, A.C.M. Ferreon, M. Arai and P.E. Wright (2010), Proc. Natl Acad. Sci., 107, (19290-19295)

 “Structure of the p53 transactivation domain in complex with the nuclear coactivator binding domain of CBP”  C.W. Lee, M. Martinez-Yamout, H.J. Dyson and P.E. Wright (2010), Biochemistry, 49, (9964-9971)

“Millisecond Timescale Fluctuations in Dihydrofolate Reductase are Exquisitely Sensitive to the Bound Ligands” D.D. Boehr, D.McElheny, H.J. Dyson and P.E. Wright (2010), Proc. Natl Acad. Sci., 107, (1373-1378)

“Energetic Frustration of Apomyoglobin Folding:  Role of the B Helix” C. Nishimura, H. J. Dyson, P.E. Wright (2010), J. Mol. Biol., 396, 1319-1328

2009

Prion proteins with pathogenic and protective mutations show similar structure and dynamics.” S.-H. Bae, G. Legname, A. Serban, S. Prusiner, P.E. Wright, H.J. Dyson (2009), Biochemistry, 48(34), 8120-8128

The Role of dynamic conformational ensembles in biomolecular recognition” D.D. Boehr, R. Nussinov, and P.E. Wright (2009), Nature Chem. Biol., 5(11), 789-796

Structural Basis for Subversion of Cellular Control Mechanisms by the Adenoviral E1A Oncoprotein” J. Ferreon, M. Martinez-Yamout, H.J. Dyson, P.E. Wright (2009), Proc. Natl Acad. Sci., 106, 13260-13265

Prediction of the Rotational Tumbling Time for Proteins with Disordered Segments” S.-H. Bae, H.J. Dyson and P.E. Wright (2009), J. Amer. Chem. Soc. 131, 6814-6821

Cooperative regulation of p53 by modulation of ternary complex formation with CBP/p300 and HDM2.” J.C. Ferreon, C.W. Lee, M. Arai, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2009) Proc. Natl Acad. Sci., USA 106, 6591-6596.

Structural basis for recruitment of CBP/p300 coactivators by STAT1 and STAT2 transactivation domains.” J.M. Wojciak, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2009) EMBO J.  28, 948-958.

“Mapping protein folding landscapes by NMR relaxation” P.E. Wright, D.J. Felitsky, K. Sugase and H.J. Dyson (2009).  In: Water and Biomolecules – Physical Chemistry of Life Phenomena (K. Kuwajima, et al., Eds.), Springer-Verlag Berlin Heidelberg, pp. 1-11.

“Functional unfolded proteins: How, when, where, and why?” H.J. Dyson, S-C Sue and P.E. Wright (2009).  In: Water and Biomolecules – Physical Chemistry of Life Phenomena (K. Kuwajima et al., Eds.), Springer-Verlag Berlin Heidelberg, pp. 123-136.

Mapping the interactions of the p53 transactivation domain with the KIX domain of CBP.” C.W. Lee, M. Arai, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2009) Biochemistry 48, 2115-2124.

Linking folding and binding.” P.E. Wright and H.J. Dyson (2009) Current Opinion in Structural Biology, 19, 31-38.

2008

The intrinsically disordered RNR inhibitor Sml1 is a dynamic dimer.” J. Danielsson, L. Liljedahl, E. Bárány-Wallje, P. Sønderby, L.H. Kristensen, M.A. Martinez-Yamout, H.J. Dyson, P.E. Wright, F.M. Poulsen, L. Mäler, A. Gräslund and B.B. Kragelund (2008) Biochemistry 47, 13428-13437.

Hierarchical folding mechanism of apomyoglobin revealed by ultra-fast H/D exchange coupled with 2D NMR.” T. Uzawa, C. Nishimura, S. Akiyama, K. Ishimori, S. Takahasi, H.J. Dyson and P.E. Wright (2008) Proc. Natl Acad. Sci, USA  105, 13859-13864.

Conformational relaxation following hydride transfer plays a limiting role in dihydrofolate reductase catalysis.” D.D. Boehr, H.J. Dyson and P.E. Wright (2008) Biochemistry 47, 9227-9233.

“How do proteins interact?” D.D. Boehr and P.E. Wright (2008) Science 320:1429-1430.

The kinetic and equilibrium molten globule intermediates of apoleghemoglobin differ in structure.” C. Nishimura, H.J. Dyson and P.E. Wright (2008) J. Mol. Biol. 378, 715-725.

Modeling transient collapsed states of an unfolded protein to provide insights into early folding events.”  D.J. Felitsky, M.A. Lietzow, H.J. Dyson and P.E. Wright (2008) Proc. Natl Acad. Sci., USA 105, 6278-6283.

NMR relaxation study of the complex formed between CBP and the activation domain of the nuclear hormone receptor coactivator ACTR.” M-O. Ebert, S-H. Bae, H.J. Dyson and P.E. Wright (2008) Biochemistry 47, 1299-1308.

Structural characterization of partially folded intermediates of apomyoglobin H64F.” S. Schwarzinger, R. Mohana-Borges, G.J.A. Kroon, H.J. Dyson and P.E. Wright (2008) Protein Sci. 17, 313-321.

Overexpression of post-translationally modified peptides in Escherichia coli by co-expression with modifying enzymes.” K. Sugase, M.A. Landes, P.E. Wright, M.A. Martinez-Yamout (2008) Protein Expr. Purif. 57, 108-115.

2007

Tailoring relaxation dispersion experiments for fast-associating protein complexes.” K. Sugase, J.C. Lansing, H.J. Dyson and P.E. Wright (2007) J. Amer. Chem. Soc. 129, 13406-13407.

Structure of the Wilms tumor suppressor protein zinc finger domain bound to DNA.” R. Stoll, B.M. Lee, E.W. Debler, J.H. Laity, I.A. Wilson, H.J. Dyson and P.E. Wright (2007), J. Mol. Biol. 372, 1227-1245.

Embryonic neural inducing factor Churchill is not a DNA-binding zinc finger protein: Solution structure reveals a solvent-exposed β-sheet and zinc binuclear cluster.” B.M. Lee, B.A. Buck-Koehntop, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2007), J. Mol. Biol. 371, 1274-1289. (Faculty of 1000 recommended paper, January, 2008).

Mechanism of coupled folding and binding of an intrinsically disordered protein.” K. Sugase, H.J. Dyson and P.E. Wright (2007), Nature 447, 1021-1027. (News & Views  by D. Eliezer and A.G. Palmer in Nature 447, 920, 2007;  Faculty of 1000 “Exceptional Paper” ; “Hot Paper”, The Scientist 23, 47, 2009).

PRAK is essential for ras-induced senescence and tumor suppression.” P. Sun, N. Yoshizuka, L. New, B.A. Moser, Y. Li, R. Liao, C. Xie, J. Chen, Q. Deng, M. Martinez-Yamout, M-Q. Dong, C.G. Frangou, J.R. Yates, P.E. Wright and J. Han (2007) Cell 128, 295-308.

2006

An NMR Perspective on Enzyme Dynamics.” D.D. Boehr, H.J. Dyson and P.E.Wright (2006), Chemical Reviews 106, 3055-3079.

Solution structure of the Hdm2 C2H2C4 RING, a domain critical for ubiquitination of p53.” M. Kostic, T. Matt, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2006) J. Mol. Biol. 363, 433-450.

The dynamic energy landscape of dihydrofolate reductase catalysis.” D.D. Boehr, D. McElheny, H.J. Dyson and P.E. Wright (2006), Science 313, 1638-1642. (Perspective by M. Vendruscolo and C.M. Dobson, Science 313, 1586, 2006;  Faculty of 1000 “Exceptional Paper”).

The role of hydrophobic interactions in initiation and propagation of protein folding.” H.J. Dyson, P.E. Wright and H.A. Scheraga (2006), Proc. Natl Acad. Sci, USA 103:13057-13061.

Localization of sites of interaction between p23 and Hsp90 in solution.” M.A. Martinez-Yamout, R.P. Venkitakrishnan, N.E. Preece, G. Kroon, P.E. Wright and H.J. Dyson (2006), J. Biol. Chem. 281, 14457-14464.

“Is there an answer? According to current textbooks, a well-defined three-dimensional structure is a prerequisite for the function of a protein. Is this correct?” H.J. Dyson and P.E. Wright (2006), IUBMB Life 58, 107-109.

Induced fit and “lock and key” recognition of 5S RNA by zinc fingers of transcription factor IIIA.” B.M. Lee, J. Xu, B.K. Clarkson, M.A. Martinez-Yamout, H.J. Dyson, D.A. Case, J.M. Gottesfeld and P.E. Wright (2006), J. Mol. Biol.  357, 275-291.

NMR solution structure of the peptide fragment 1-30, derived from unprocessed mouse Doppel protein, in DHPC micelles.” E. Papadopoulos, K. Oglecka, L. Mäler, J. Jarver, P.E. Wright, H.J. Dyson, and A. Gräslund (2006), Biochemistry 45, 159-166.

Structural basis for cooperative transcription factor binding to the CBP coactivator.” R.N. De Guzman, N.K. Goto, H.J. Dyson and P.E. Wright (2006), J. Mol. Biol.  355, 1005-1013.

Structure of the Escherichia coli quorum sensing protein SdiA: Activation of the folding switch by acyl homoserine lactones.” Y. Yao, M.A. Martinez-Yamout, T.J. Dickerson, A.P. Brogan, P.E. Wright and H.J. Dyson (2006), J. Mol. Biol. 355, 262-273.

Identification of native and non-native structure in kinetic folding intermediates of apomyoglobin.” C. Nishimura, H.J. Dyson and P.E. Wright (2006), J. Mol. Biol. 355, 139-156.

2005

Solution structure of the N-terminal zinc fingers of the xenopus laevis double-stranded RNA-binding protein ZFa.” H.M. Möller, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2005), J. Mol. Biol. 351, 718-730.

Sequence determinants of a protein folding pathway.” C. Nishimura, M.A. Lietzow, H.J. Dyson and P.E. Wright (2005), J. Mol. Biol. 351, 383-392.

Elucidation of the protein folding landscape by NMR.” H.J. Dyson and P.E. Wright (2005) In: Methods in Enzymology, (Thomas L. James, Ed.) Elsevier, Inc. 394, 299-321.

Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis.” D. McElheny, J.R. Schnell, J.C. Lansing, H.J. Dyson and P.E. Wright (2005), Proc. Natl Acad. Sci., USA 102, 5032-5037. (Faculty of 1000 “Must Read” paper, May 2005).

Enhanced picture of protein-folding intermediates using organic solvents in H/D exchange and quench-flow experiments.” C. Nishimura, H.J. Dyson and P.E. Wright (2005), Proc. Natl Acad. Sci., USA 102, 4765-4770.

Inhibition of DNA binding by human estrogen related receptor-2 and estrogen receptor α with minor groove-binding polyamides.” M.D. Gearhart, L. Dickinson, J. Ehley, C. Melander, P.B. Dervan, P.E. Wright and J.M. Gottesfeld (2005),  Biochemistry 44, 4196-4203.

Intrinsically unstructured proteins and their function.” H.J. Dyson and P.E. Wright (2005) Nature Rev. Mol. Cell Biol., 6, 197-208. (Highlighted in ESI Special Topics, February 2006, as a “Fast Breaking Paper”.  http:/esi-topics.com).

CBP/p300 TAZ1 domain forms a structural scaffold for ligand binding.” R.N. De Guzman, J.M. Wojciak, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2005), Biochemistry 44, 490-497.

2004

ZZ domain of CBP: an unusual zinc finger fold in a protein interaction module.”  G.B. Legge, M.A. Martinez-Yamout, D.M. Hambly, T. Trinh, B.M. Lee, H.J. Dyson and P.E. Wright (2004), J. Mol. Biol. 343, 1081-1093.

“Structure and function of the CBP/p300 TAZ domains.” R.N. De Guzman, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2004) In: Zinc Finger Proteins: From Atomic Contact to Cellular Function, Eds. S. Iuchi, N. Kuldell, Landes Bioscience, Georgetown, TX  17, 114-122.

Conformational changes in the active site loops of dihydrofolate reductase during the catalytic cycle.” R.P. Venkitakrishnan, E. Zaborowski, D. McElheny, S.J. Benkovic, H.J. Dyson and P.E. Wright (2004), Biochemistry, 43, 16046-16055.

Unfolded proteins and protein folding studied by NMR.” H.J. Dyson and P.E. Wright (2004) Chemical Reviews, 104, 3607-3622.

Thematic issue: “Biological Nuclear Magnetic Resonance.” H.J. Dyson and P.E. Wright, Guest Editors (2004) Chemical Reviews 104, pp. 3517-3704.

Structural characterization of unfolded states of apomyoglobin using residual dipolar couplings.” R. Mohana-Borges, N.K. Goto, G.J.A. Kroon, H.J. Dyson and P.E. Wright (2004) J. Mol. Biol., 340, 1131-1142.

The CBP/p300 TAZ1 domain in its native state is not a binding partner of MDM2.” T. Matt, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2004) Biochem. J., 381, 685-691.  (Commentary: Biochem. J. 381, e3-e4, 2004; Faculty of 1000 “Must Read” paper, August 2004).

The LEF-1 high-mobility group domain undergoes a disorder-to-order transition upon formation of a complex with cognate DNA.” J.J. Love, X. Li, J. Chung, H.J. Dyson and P.E. Wright (2004) Biochemistry, 43, 8725-8734.

Model-free analysis of protein dynamics: assessment of accuracy and model selection protocols based on molecular dynamics simulation.” J. Chen, C.L. Brooks, III and P.E. Wright (2004)  J. Biomolecular NMR, 29, 243-257.

Structure, dynamics and catalytic function of dihydrofolate reductase.”  J.R. Schnell, H.J. Dyson and P.E. Wright (2004) Ann. Rev. Biophys. Biomol. Struct., 33, 119-140.

Solution structure of the KIX domain of CBP bound to the transactivation domain of c-Myb.” T. Zor, R.N. De Guzman, H.J. Dyson and P.E. Wright (2004) J. Mol. Biol., 337, 521-534.

Recognition of the mRNA AU-rich element by the zinc finger domain of TIS11d.” B.P. Hudson, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2004) Nat. Struct. Biol., 11, 257-264.

Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: Regulation by competition between intrinsically unstructured ligands for non-identical binding sites.” R.N. De Guzman, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2004) J. Biol. Chem., 279, 3042-3049.

Effect of cofactor binding and loop conformation on side chain methyl dynamics in dihydrofolate reductase.” J.R. Schnell, H.J. Dyson and P.E. Wright (2004) Biochemistry, 43, 374-383.

Packing, specificity and mutability at the binding interface between the p160 coactivator and CREB-binding protein.” S.J. Demarest, S. Deechongkit, H.J. Dyson, R.M. Evans and P.E. Wright (2004) Protein Science, 13, 203-210.

2003

Role of the B helix in early folding events in apomyoglobin: Evidence from site-directed mutagenesis for native-like long range interactions.” C. Nishimura, P.E. Wright and H.J. Dyson (2003) J. Mol. Biol., 334, 293-307.

Diagnostic chemical shift markers for loop conformation and substrate and cofactor binding in dihydrofolate reductase complexes.” M.J. Osborne, R.P. Venkitakrishnan, H.J. Dyson and P.E. Wright (2003) Protein Science, 12, 2230-2238.

Changes in structure and dynamics of the Fv fragment of a catalytic antibody upon binding of inhibitor.” G.J.A. Kroon, H. Mo, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2003) Protein Science, 12, 1386-1394.

Role of a solvent-exposed tryptophan in the recognition and binding of antibiotic substrates for a metallo-β-lactamase.” J.J.A. Huntley, W. Fast, S.J. Benkovic, P.E. Wright and H.J. Dyson (2003) Protein Science, 12, 1368-1375.

Structure of the nuclear factor ALY: Insights into post-transcriptional regulatory and mRNA nuclear export processes.” G.C. Perez-Alvarado, M. Martinez-Yamout, M.M. Allen, R. Grosschedl, H.J. Dyson and P.E. Wright (2003) Biochemistry, 42, 7348-7357.

Folding of a β-sheet protein monitored by real-time NMR spectroscopy.”  M. Mizuguchi, G.J. Kroon, P.E. Wright and H.J. Dyson (2003) J. Mol. Biol., 328, 1161-1171.

Monomeric complex of human orphan estrogen related receptor-2 with DNA: A pseudo-dimer interface mediates extended half-site recognition.” M.D. Gearhart, S.M.A. Holmbeck, R.M. Evans, H.J. Dyson and P.E. Wright (2003) J. Mol. Biol., 327, 819-832.

2002

Cooperativity in transcription factor binding to the coactivator CREB-binding Protein (CBP).” N.K. Goto, T. Zor, M. Martinez-Yamout, H.J. Dyson and P.E. Wright (2002) J. Biol. Chem., 277, 43168-43174.

Insights into the structure and dynamics of unfolded proteins from nuclear magnetic resonance.”  H. Jane Dyson and P.E. Wright (2002) Adv. in Protein Chem., 62, 311-40.

Roles of phosphorylation and helix propensity in the binding of the KIX domain of CREB-binding protein by constitutive (c-Myb) and inducible (CREB) activators.” T. Zor, B.M. Mayr, H.J. Dyson, M.R. Montminy and P.E. Wright (2002) J. Biol. Chem., 277, 42241-42248.

The apomyoglobin folding pathway revisited: Structural heterogeneity in the kinetic burst phase intermediate.” C. Nishimura, H.J. Dyson and P.E. Wright (2002) J. Mol. Biol., 322, 483-489.

Molecular hinges in protein folding: the urea-denatured state of apomyoglobin.” S. Schwarzinger, P.E. Wright and H.J. Dyson (2002) Biochemistry, 41, 12681-12686.

Mapping long-range contacts in a highly unfolded protein.” M.A. Lietzow, M. Jamin, H.J. Dyson and P.E. Wright (2002) J. Mol. Biol., 322, 655-662.

High pressure NMR reveals that apomyoglobin is an equilibrium mixture from the native to the unfolded.” R. Kitahara, H. Yamada, K. Akasaka and P.E. Wright (2002) J. Mol. Biol., 320, 311-319.

“Structure and dynamics of disordered proteins.”  H.J. Dyson and P.E. Wright (2002)  In:  Encyclopedia of NMR, (D.M. Grant & R.K. Harris, eds.), John Wiley & Sons, Ltd.,  9, 449-457.

Comparison of protein solution structures refined by molecular dynamics simulation in vacuum, with a generalized Born model, and with explicit water.” B. Xia, V. Tsui, D.A. Case, H.J. Dyson and P.E. Wright (2002), J. Biomol. NMR, 22, 317-331.

“Assignment of a 15 kDa protein complex formed between the p160 coactivator ACTR and CREB binding protein.” S.J. Demarest, J. Chung, H.J. Dyson and P.E. Wright (2002) J. Biomol. NMR, 22, 377-378.

Structural basis for Hif-1α/CBP recognition in the cellular hypoxic response.”  S.A. Dames, M. Martinez-Yamout, R.N. De Guzman, H.J. Dyson and P.E. Wright (2002) Proc. Natl Acad. Sci, USA, 99, 5271-5276. (Faculty of 1000 “Must Read” paper, May 2002).

Solution NMR spectroscopy of [α-15N]lysine-labeled rhodopsin: The single peak observed in both conventional and TROSY-type HSQC spectra is ascribed to Lys-339 in the carboxyl-terminal peptide sequence.” J. Klein-Seetharaman, P.J. Reeves, M.C. Loewen, E.V. Getmanova, J. Chung, H. Schwalbe, P.E. Wright and H.G. Khorana (2002) Proc. Natl Acad. Sci, USA, 99, 3452-3457.

Coupling of folding and binding for unstructured proteins.”  H.J. Dyson and P.E. Wright (2002) Curr. Opin. Struct. Biol., 12, 54-60.

Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators.”  S.J. Demarest, M. Martinez-Yamout, J. Chung, H. Chen, W. Xu, H.J. Dyson, R.M. Evans and P.E. Wright (2002) Nature, 415, 549-553.

2001

Conformational and dynamic characterization of the molten globule state of an apomyoglobin mutant with an altered folding pathway.” S. Cavagnero, C. Nishimura, S. Schwarzinger, H.J. Dyson and P.E. Wright (2001) Biochemistry, 40, 14459-14467.

“Potential bias in NMR relaxation data introduced by peak intensity analysis and curve fitting methods.” J.H. Viles, B.M. Duggan, E. Zaborowski, S. Schwarzinger, J.J.A. Huntley, G.J.A. Kroon, H.J. Dyson and P.E. Wright (2001) J. Biomol. NMR, 21, 1-9.

Backbone dynamics in dihydrofolate reductase complexes:  Role of loop flexibility in the catalytic mechanism.” M.J. Osborne, J. Schnell, S.J. Benkovic, H.J. Dyson and P.E. Wright (2001)  Biochemistry, 40, 9846-9859. (Faculty of 1000 “Recommended” paper, October 2001).

Solution structure of the third immunoglobulin domain of the neural cell adhesion molecule N-CAM: Can solution studies define the mechanism of homophilic binding?”  A.R. Atkins, J. Chung, S-P. Deechongkit, E.B. Little, G.M. Edelman, P.E. Wright, B.A. Cunningham and H.J. Dyson (2001)  J. Mol. Biol., 311, 161-172.

Solution structure of Escherichia coli glutaredoxin-2 shows similarity to mammalian glutathione-S-transferases.” B. Xia, A. Vlamis-Gardikas, A. Holmgren, P.E. Wright and H.J. Dyson (2001) J. Mol. Biol., 310, 907-918.

“Nuclear magnetic resonance methods for the elucidation of structure and dynamics in disordered states.” H.J. Dyson and P.E. Wright (2001)  In:  Methods in Enzymology,  (T.L. James, V. Dötsch, and U. Schmitz, eds.), Academic Press, San Diego  339, 258-270.

Structural and dynamic characterization of an unfolded state of poplar apo-plastocyanin formed under non-denaturing conditions.” Y. Bai, J. Chung, H.J. Dyson and P.E. Wright (2001) Protein Science, 10, 1056-1066.

NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding.”   J. Yao, J. Chung, D. Eliezer, P.E. Wright and H.J. Dyson (2001) Biochemistry, 40, 3561-3571.

“SANE (structure assisted NOE evaluation): An automated model-based approach for NOE assignment.”  B.M. Duggan, G.B. Legge, H.J. Dyson and P.E. Wright (2001) J. Biomol. NMR, 19, 321-329.

Sequence-dependent correction of random coil NMR chemical shifts.”  S. Schwarzinger, G.J.A. Kroon, T.R. Foss, J. Chung, P.E. Wright and H.J. Dyson (2001)  J. Amer. Chem. Soc., 123, 2970-2978.

Anisotropic rotational diffusion in model-free analysis for a ternary-DHFR complex.”  M.J. Osborne and P.E. Wright (2001) J. Biomol. NMR, 19, 209-230.

Two different neurodegenerative diseases caused by proteins with similar structures.”  H. Mo, R.C. Moore, F.E. Cohen, D. Westaway, S.B. Prusiner, P.E. Wright and H.J. Dyson (2001) Proc. Natl Acad. Sci, USA, 98, 2352-2357.

Local structural plasticity of the prion protein. Analysis of NMR relaxation dynamics.”  J.H. Viles, D. Donne, G. Kroon, S.B. Prusiner, F.E. Cohen, H.J. Dyson and P.E. Wright (2001) Biochemistry, 40, 2743-2753.

Zinc finger proteins:  New insights into structural and functional diversity.”  J.H. Laity, B.M. Lee and P.E. Wright  (2001) Curr. Opin. Struct. Biol., 11, 39-46.

2000

Dynamics of the metallo-ß-lactamase from Bacteroides fragilis in the presence and absence of a tight-binding inhibitor.” J.J.A. Huntley, S.D.B. Scrofani, M.J. Osborne, P.E. Wright and H.J. Dyson (2000) Biochemistry, 39, 13356-13364.

Structure of the PHD zinc finger from human Williams-Beuren Syndrome transcription factor.”  J. Pascual, M. Martinez-Yamout, H.J. Dyson and P.E. Wright (2000) J. Mol. Biol., 304, 723-729.

Molecular basis for modulation of biological function by alternate splicing of the Wilms’ tumor suppressor protein.” J.H. Laity, H.J. Dyson and P.E. Wright (2000)  Proc. Natl Acad. Sci, USA, 97, 11932-11935.

Random coil chemical shifts in acidic 8 M urea: Implementation of random coil shift data in NMRview.” S. Schwarzinger, G.J.A. Kroon, T.R. Foss, P.E. Wright, H.J. Dyson (2000) J. Biomol. NMR, 18, 43-48.

Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain.” B.P. Hudson, M.A. Martinez-Yamout, H.J. Dyson and P.E. Wright (2000) J. Mol. Biol., 304, 355-370.

Changes in the apomyoglobin folding pathway caused by mutation of the distal histidine residue.” C. Garcia, C. Nishimura, S. Cavagnero, H.J. Dyson and P.E. Wright (2000) Biochemistry, 39, 11227-11237.

Solution structure of the TAZ2 (CH3) domain of the transcriptional adaptor protein CBP.”  R.N. De Guzman, H.Y. Liu, M. Martinez-Yamout, H.J. Dyson and P.E. Wright (2000) J. Mol. Biol., 303, 243-253.

NMR and molecular dynamics studies of the hydration of a zinc finger-DNA complex.” V. Tsui, I. Radhakrishnan, P.E. Wright and D.A. Case (2000) J. Mol. Biol., 302, 1101-1117.

Conservation of folding pathways in evolutionarily distant globin sequences.” C. Nishimura, S. Prytulla, H.J. Dyson and P.E. Wright (2000) Nat. Struct. Biol., 7, 679-686.

Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJ.” M. Martinez-Yamout, G.B. Legge, O. Zhang, P.E. Wright and H.J. Dyson (2000) J. Mol. Biol., 300, 805-818.

Backbone HN, N, Ca, C and Cb assignments of the 19 kDa DHFR/NADPH complex at 9oC and pH 7.6.”  E. Zaborowski, J. Chung, G. Kroon, H.J. Dyson and P.E. Wright (2000) J. Biomol. NMR, 16, 349-350.

Alternative splicing of Wilms’ tumor suppressor protein modulates DNA binding activity through isoform-specific DNA-induced conformational changes.”  J.H. Laity, J. Chung, H.J. Dyson and P.E. Wright (2000) Biochemistry, 39, 5341-5348.

Assignment of 1H, 13C and 15N resonances of the I-domain of human leukocyte function associated antigen-1.” R.W. Kriwacki, G.B. Legge, U. Hommel, P. Ramage, J. Chung, L.L. Tennant, P.E. Wright and H.J. Dyson (2000) J. Biomol. NMR, 16, 271-272.

Identification of the regions involved in DNA-binding by the mouse PEBP2α protein.” G.C. Perez-Alvarado, A. Munnerlyn, H.J. Dyson, R. Grosschedl and P.E. Wright (2000) FEBS Letters, 470, 125-130.

Native and non-native secondary structure and dynamics in the pH 4 intermediate of apomyoglobin.”  D. Eliezer, J. Chung, H.J. Dyson and P.E. Wright (2000) Biochemistry, 39, 2894-2901.

Assessment of zinc finger orientations by residual dipolar coupling constants.”  V. Tsui, L. Zhu, T-H. Huang, P.E. Wright and D.A. Case (2000) J. Biomol. NMR, 16, 9-21.

Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15N-1H NMR spectra.”  S. Cavagnero, Y. Thériault, S. Narula, H.J. Dyson and P.E. Wright (2000) Protein Sci., 9, 186-193.

DNA-induced a-helix capping in conserved linker sequences is a determinant of binding affinity in Cys2-His2 zinc fingers.” J.H. Laity, H.J. Dyson and P.E. Wright (2000) J. Mol. Biol., 295, 719-727.

“NMR solution structure of the inserted domain of human leukocyte function associated antigen-1.” G.B. Legge, R.W. Kriwacki, J. Chung, U. Hommel, P. Ramage, D.A. Case, H.J. Dyson and P.E. Wright (2000) J. Mol. Biol., 295, 1251-1264.

1999

Determination of Fe-ligand bond lengths and the Fe-N-O bond angles in soybean ferrous and ferric nitrosylleghemoglobin a using multiple-scattering XAFS analyses.” A.M. Rich, P.J. Ellis, L. Tennant, P.E. Wright, R.S. Armstrong and P.A. Lay (1999) Biochemistry, 38, 16491-16499.

NMR characterization of the metallo-ß-lactamase from bacteroides fragilis and its interaction with a tight-binding inhibitor: Role of an active site loop.” S.D.B. Scrofani, J. Chung, J.J.A. Huntley, S.J. Benkovic, P.E. Wright and H.J. Dyson (1999) Biochemistry, 38, 14507-14514.

Inherent flexibility in a potent inhibitor of blood coagulation, recombinant nematode anticoagulant protein c2.” B.M. Duggan, H.J. Dyson and P.E. Wright (1999) Eur. J. Biochem. 265, 539-548.

Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm.”  P.E. Wright and H.J. Dyson (1999) J. Mol. Biol. 293, 321-331.

Characterization of monomeric and dimeric B domain of staphylococcal protein A: Sources of stabilization of a 3-helix bundle protein.” A. Karimi, M. Matsumura, P.E. Wright and H.J. Dyson (1999) J. Pept. Res. 54, 344-352.

“Assignment of 1H, 13C, and 15N resonances of reduced Escherichia coli glutaredoxin 2.”  B. Xia, J. Chung, A. Vlamis-Gardikas, A. Holmgren, P.E. Wright and H.J. Dyson (1999) J. Biomol. NMR 14, 197-198.

Backbone resonance assignments for the Fv fragment of the catalytic antibody NPN43C9 with bound p-nitrophenol.”  G.J.A. Kroon, M.A. Martinez-Yamout, J.F. Krebs, J. Chung, H.J. Dyson and P.E. Wright (1999) J. Biomol. NMR 15, 83-84.

Identification of a minimal domain of 5S ribosomal RNA sufficient for high affinity interactions with the RNA-specific zinc fingers of transcription factor IIIA.”  L.S. Neely, B.M. Lee, J. Xu, P.E. Wright and J.M. Gottesfeld (1999) J. Mol. Biol. 291, 549-560.

Role of secondary structure in discrimination between constitutive and inducible activators.” D. Parker, M. Rivera, T. Zor, A. Henrion-Caude, I. Radhakrishnan, A. Kumar, L.H. Shapiro, P.E. Wright, M. Montminy and P.K. Brindle (1999) Mol. Cell. Biol.  19, 5601-5607.

Association between the first two immunoglobulin-like domains of the neural cell adhesion molecule N-CAM.”  A.R. Atkins, M.J. Osborne, H.A. Lashuel, G.M. Edelman, P.E. Wright, B.A. Cunningham and H.J. Dyson (1999) FEBS Lett.  451, 162-168.

Improved low pH bicelle system for orienting macromolecules over a wide temperature range.” S. Cavagnero, H.J. Dyson and P.E. Wright (1999) J. Biomol. NMR 13, 387-391.

Structural analyses of CREB-CBP transcriptional activator-coactivator complexes by NMR spectroscopy: Implications for mapping the boundaries of structural domains.” I. Radhakrishnan, G.C. Perez-Alvarado, D. Parker, H.J. Dyson, M. Montminy and P.E. Wright (1999) J. Mol. Biol. 287, 859-865.

Copper binding to the prion protein: Structural implications of four identical cooperative binding sites.” J.H. Viles, F.E. Cohen, S.B. Prusiner, D.B. Goodin, P.E. Wright and H.J. Dyson (1999) Proc. Natl Acad. Sci., USA  96, 2042-2047.

Quench-flow experiments combined with mass spectrometry show apomyoglobin folds through an obligatory intermediate.” V. Tsui, C. Garcia, S. Cavagnero, G. Siuzdak, H.J. Dyson and P.E. Wright (1999) Protein Sci.  8, 45-49.

Effect of H helix destabilizing mutations on the kinetic and equilibrium folding of apomyoglobin.” S. Cavagnero, H.J. Dyson, P.E. Wright (1999) J. Mol. Biol. 285, 269-282.

1998

DNA-induced conformational changes are the basis for cooperative dimerization by the DNA binding domain of the retinoid-X-receptor.” S.M.A. Holmbeck, H.J. Dyson and P.E. Wright (1998) J. Mol. Biol. 284, 533-539.

The identification of metal-binding ligand residues in metalloproteins using nuclear magnetic resonance spectroscopy.” S.D.B. Scrofani, P.E. Wright and H.J. Dyson (1998) Protein Sci. 7, 2476-2479.

Analysis of an activator:Coactivator complex reveals an essential role for secondary structure in transcriptional activation.” D. Parker, U. Jhala, I. Radhakrishnan, M.B. Yaffe, C. Reyes, A.I. Shulman, L.C. Cantley, P.E. Wright and M. Montminy (1998).  Mol. Cell 2, 353-359.

Sequence requirements for stabilization of a peptide reverse turn in water solution: proline is not essential for stability.” H.J. Dyson, L. Bolinger, V.A. Feher, J.J. Osterhout, Jr., J. Yao and P.E. Wright (1998) Eur. J. Biochem. 255, 462-471.

1H, 13C and 15N NMR backbone assignments of 25.5 kDa metallo-b-lactamase from bacteroides fragilis.”  S.D.B. Scrofani, P.E. Wright and H.J. Dyson (1998) J. Biomol. NMR 12, 201-202.

Chemical shift as a probe of molecular interfaces: NMR studies of DNA binding by three amino-terminal zinc finger domains from transcription factor IIIA.”  M.P. Foster, D.S. Wuttke, K.R. Clemens, W. Jahnke, I. Radhakrishnan, L. Tennant, M. Reymond, J. Chung and P.E. Wright (1998) J. Biomol. NMR 12, 51-71.

High resolution solution structure of the retinoid X receptor DNA binding domain.”  S.M.A. Holmbeck, M.P. Foster, D.R. Casimiro, D. Sem, H.J. Dyson and P.E. Wright (1998) J. Mol. Biol. 281, 271-284.

Distributed torsion angle grid search in high dimensions:  A systematic approach to NMR structure determination.”  G.P. Gippert, P.E. Wright and D.A. Case (1998) J. Biomol. NMR 11, 241-263.

Equilibrium NMR studies of unfolded and partially folded proteins.”  H.J. Dyson and P.E. Wright (1998) Nat. Struct. Biol. 5, 499-503.

Conformational preferences in the Ser133-phosphorylated and non-phosphorylated forms of the kinase inducible transactivation domain of CREB.”  I. Radhakrishnan, G.C. Perez-Alvarado, H.J. Dyson and P.E. Wright (1998)  FEBS Lett. 430, 317-322.

Recommendations for the presentation of NMR structures of proteins and nucleic acids.” J.L. Markley, A. Bax, Y. Arata, C.W. Hilbers, R. Kaptein, B.D. Sykes, P.E. Wright and K. Wüthrich (1998)  Pure Appl. Chem. 70, 117-142.

High-resolution solution structure of Bacillus subtilis IIAglc .”  Y. Chen, D.A. Case, J. Reizer, M.H. Saier, Jr. and P.E. Wright (1998)  Proteins: Structure, Function and Genetics 31, 258-270.

A NOESY-HSQC simulation program, SPIRIT.” L. Zhu, H.J. Dyson and P.E. Wright (1998) J. Biomol. NMR 11, 17-29.

Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding.” D. Eliezer, J. Yao, H.J. Dyson and P.E. Wright (1998) Nat. Struct. Biol.  5, 148-155.

1997

Chemical shift dispersion and secondary structure prediction in unfolded and partly-folded proteins.”  J. Yao, H.J. Dyson and P.E. Wright (1997) FEBS Lett. 419, 285-289.

Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: A model for activator:coactivator interactions.” I. Radhakrishnan, G.C. Perez-Alvarado, H.J. Dyson, D. Parker, M.R. Montminy and P.E. Wright (1997) Cell  91, 741-752.

Structure of the recombinant full-length hamster prion protein PrP (29-231): The N-terminus is highly flexible.”  D.G. Donne, J.H. Viles, D. Groth, I. Melhorn, T.L. James, F.E. Cohen, S.B. Prusiner, P.E. Wright and H.J. Dyson (1997)  Proc. Natl Acad. Sci., USA  94, 13452-13457.

PCR-based gene synthesis and protein NMR spectroscopy.”  D.R. Casimiro, P.E. Wright and H.J. Dyson  (1997)  Struct. 5, 1407-1412.

Probing protein structure using biochemical and biophysical methods: Proteolysis, matrix-assisted laser desorption/ionization mass spectrometry, high-performance liquid chromatography and size-exclusion chromatography of p21Wafl/Cipl/Sdi1.”  R.W. Kriwacki, J. Wu, L. Tennant, P.E. Wright and G. Siuzdak (1997) J. Chrom. A  777, 23-30.

Populating the equilibrium molten globule state of apomyoglobin under conditions suitable for structural characterization by NMR.”  D. Eliezer, P.A. Jennings, H.J. Dyson and P.E. Wright (1997) FEBS Lett. 417, 92-96.

Solution structure of the first three zinc fingers of TFIIIA bound to the cognate DNA sequence:  Determinants of affinity and sequence specificity.”  D.S. Wuttke, M.P. Foster, D.A. Case, J.M. Gottesfeld and P.E. Wright (1997) J. Mol. Biol.  273, 183-206.

Domain packing and dynamics in the DNA complex of the N-terminal zinc fingers of TFIIIA.” M.P. Foster, D.S. Wuttke, I. Radhakrishnan, D.A. Case, J.M. Gottesfeld and P.E. Wright (1997) Nat. Struct. Biol. 4, 605-608.

NMR spectroscopic studies of the DNA-binding domain of the monomer-binding nuclear orphan receptor, human estrogen related receptor-2.  The carboxy-terminal extension to the zinc-finger region is unstructured in the free form of the protein.” D.S. Sem, D.R. Casimiro, S.A. Kliewer, J. Provencal, R.M. Evans and P.E. Wright (1997) J. Biol. Chem. 272, 18038-18043.

Absence of a stable intermediate on the folding pathway of protein A.”  Y. Bai, A. Karimi, H.J. Dyson and P.E. Wright (1997) Protein Sci.  6, 1449-1457.

Contribution of increased length and intact capping sequences to the conformational preference for helix in a 31-residue peptide from the C-terminus of myohemerythrin.” M.T. Reymond, S. Huo, B. Duggan, P.E. Wright and H.J. Dyson (1997) Biochemistry 36, 5234-5244.

Folding propensities of peptide fragments of myoglobin.” M.T. Reymond, G. Merutka, H.J. Dyson and P.E. Wright (1997) Protein Sci. 6, 706-716.

1996

Gene synthesis, high level expression and assignment of backbone 15N and 13C resonances of soybean leghemoglobin.” S. Prytulla, H.J. Dyson and P.E. Wright (1996) FEBS Lett. 399, 283-289.

Is apomyoglobin a molten globule?  Structural characterization by NMR.”  D. Eliezer and P.E. Wright (1996) J. Mol. Biol.  263, 531-538.

Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: Conformational disorder mediates binding diversity.”  R.W. Kriwacki, L. Hengst, L. Tennant, S.I. Reed and P.E. Wright (1996)  Proc. Natl Acad. Sci. USA 93, 11504-11509.

“Biophysical methods: Faster and bigger.” P.E. Wright and J.L. Smith (1996) Cur. Opin. Struct. Biol. 6, 583-584.

“Determination of the structures of proteins and protein complexes in solution using NMR.” P.E. Wright, M. Foster, X. Li, J. Love and D. Wuttke (1996) BioJapan ’96, Symp. Proc. 401-408.

Assessment of major and minor groove DNA interactions by the zinc fingers of Xenopus transcription factor IIIA.” S.J. McBryant, B. Gedulin, K.R. Clemens, P.E. Wright and J.M. Gottesfeld (1996) Nucl. Acids Res.  24, 2567-2574.

Insights into protein folding from NMR.”  H.J. Dyson and P.E. Wright (1996) Ann. Rev. Phys. Chem. 47, 369-395.

“Probing protein/protein interactions with mass spectrometry and isotopic labeling: Analysis of the p21/Cdk2 complex.”  R.W. Kriwacki, J. Wu, G. Suizdak and P.E. Wright (1996) J. Am. Chem. Soc. 118, 5320-5321.

Hydrogen exchange in the carbon monoxide complex of soybean leghemoglobin.”  D. Morikis and P.E. Wright, (1996) Eur. J. Biochem. 237, 212-220.

“NMR structural studies of flexible molecules.”  P.E. Wright and H.J. Dyson (1996) In: NMR as a Structural Tool for Macromolecules (B.D. Nageswara Rao and M.D. Kemple, Eds) Plenum Publishing Corp., New York, pp. 245-249.

“Proteins & Protein Fragments:  Folding.”  H.J. Dyson and P.E. Wright (1996) In: Encyclopedia of NMR, (D.M. Grant and R.K. Harris, Eds.), Wiley, New York  pp. 3811-3820.

1995

Overexpression of myoglobin and assignment of it’s amide, Ca and Cb resonances.”  P.A. Jennings, M.J. Stone and P.E. Wright (1995) J. Biomol. NMR 6, 271-276.

Structural basis for DNA bending by the architectural transcription factor LEF-1.” J.J. Love, X. Li, D.A. Case, K. Giese, R. Grosschedl and P.E. Wright (1995) Nature 376, 791-795.

The radius of gyration of an apomyoglobin folding intermediate.”  D. Eliezer, P.A. Jennings, P.E. Wright, S. Doniach, K.O. Hodgson and H. Tsuruta (1995) Science 270, 487-488.

Dynamics of the dihydrofolate reductase-folate complex: Catalytic sites and regions known to undergo conformational change exhibit diverse dynamical features.”  D.M. Epstein, S.J. Benkovic and P.E. Wright (1995) Biochemistry, 34, 11037-11048.

Measurement of intrinsic exchange rates of amide protons in a 15N-labeled peptide.”  S. Koide, W. Jahnke and  P.E. Wright (1995) J. Biomol. NMR, 6, 306-312.

Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling.”  R. Brüschweiler, X. Liao and P.E. Wright (1995) Science 268, 886-889.

Recombinant soluble human tissue factor secreted by Saccharomyces cerevisiae and refolded from E.coli inclusion bodies: glycosylation of mutants, activity and physical characterization.”  M.J. Stone, W. Ruf, D.J. Miles, T.S. Edgington and  P.E. Wright (1995) Biochem. J., 310, (Part 2), 605-614.

Interaction of the RNA binding fingers of Xenopus transcription factor IIIA with specific regions of 5S ribosomal RNA.”  S.J. McBryant, B. Gedulin, A. Leresche, M.P. Foster,  P.E. Wright, P.J. Romaniuk and J.M. Gottesfeld (1995) J. Mol. Biol., 248, 44-57.

“Isotope labeling for NMR studies of macromolecular structure and interactions.”   P.E. Wright (1994) Stable Isotope Applications in Biomolecular Structure and Mechanisms, Eds. J. Trewhella, T.A. Cross, C.J. Unkefer, Los Alamos National Laboratory, Los Alamos, 1-11.

Hydration of the partially folded peptide RN-24 studied by multi-dimensional NMR.”  R. Brüschweiler, D. Morikis and P.E. Wright (1995) J Biomol. NMR, 5, 353-356.

“‘Random coil’ 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG.”  G. Merutka, H.J. Dyson and P.E. Wright, (1995) J. Biomol. NMR, 5, 14-24.

Antigenic peptides.”  H.J. Dyson and P.E. Wright (1995) FASEB J., 9, 37-42.

1994

“Water self-diffusion model for protein-water NMR cross relaxation.”  R. Brüschweiler and P.E. Wright (1994) Chem. Phys. Lett. 229, 75-81.

“Differential side chain hydration in a linear peptide containing a type VI turn.”  J. Yao, R. Brüschweiler, H.J. Dyson and P.E. Wright (1994) J. Am. Chem. Soc., 116, 12051-12052.

Three-dimensional structure of a type VI turn in a linear peptide in water solution:  Evidence for stacking of aromatic rings as a major stabilizing factor.”  J. Yao, H.J. Dyson and P.E. Wright (1994) J. Mol. Biol., 243, 754-766.

Stabilization of a type VI turn in a family of linear peptides in water solution.”  J. Yao, V.A. Feher, F. Espejo, M.T. Reymond, P.E. Wright and H.J. Dyson (1994) J. Mol. Biol., 243, 736-753.

“NMR order parameters of biomolecules:  A new analytical representation and application to the Gaussian axial fluctuation model.”  R. Brüschweiler and P.E. Wright (1994) J. Am.Chem. Soc., 116, 8426-8427.

Relative contributions of the zinc fingers of transcription factor IIIA to the energetics of DNA binding.”  K.R. Clemens, P. Zhang, X. Liao, S.J. McBryant, P.E. Wright and J.M. Gottesfeld (1994) J. Mol. Biol., 244, 23-35.

Solution structure of carbonmonoxy myoglobin determined from NMR distance and chemical shift constraints.”  K. Ösapay, Y. Theriault, P.E. Wright and D.A. Case (1994) J. Mol. Biol., 244, 183-197.

High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin.”  M-F. Jeng, A.P. Campbell, T. Begley, A. Holmgren, D.A. Case, P.E. Wright and H.J. Dyson (1994) Struct., 2, 853-868.

NMR assignments and secondary structure of the retinoid X receptor a DNA-binding domain:  Evidence for the novel C-terminal helix.”  M.S. Lee, D.S. Sem, S.A. Kliewer, J. Provencal, R.M. Evans and P.E. Wright (1994) Eur. J. Biochem., 224, 639-650.

“Protein structure calculation using NMR restraints.”  H.J. Dyson and P.E. Wright (1994) In: “Two-dimensional NMR spectroscopy: Applications for chemists and biochemists,” Eds. W.R. Croasmun and R. Carlson, VCH, New York, 655-698.

“Use of chemical shifts and coupling constants in NMR structural studies on peptides and proteins.”  D.A. Case, H.J. Dyson and P.E. Wright (1994) In: “Methods in Enzymology,” 239, 392-416.

“The folding pathway of apomyoglobin.”  P.A. Jennings, H.J. Dyson and P.E. Wright (1994) In: Statistical Mechanics, Protein Structure, and Protein Substrate Interactions, NATO ARW, Ed. S. Doniach, Plenum Press, New York, 7-18.

“Detecting nascent structures in solution using NMR.”  H.J. Dyson, J. Yao, and P.E. Wright (1994) In: “Proceedings of the 13th American Peptide Symposium.  Peptides:  Chemistry, Structure, and Biology” Eds. R.S. Hodges and J.A. Smith, ESCOM, Leiden, The Netherlands, 1093-1095.

“1H and 15N resonance assignments and secondary structure of  the carbon monoxide complex of sperm whale myoglobin.”  Y. Theriault, T.C. Pochapsky, C. Dalvit, M. Chiu, S.G. Sligar and P.E. Wright (1994) J. Biomol. NMR, 4, 491‑504.

“1H, 15N and 13C resonance assignments for the first three zinc fingers of transcription factor IIIA.”  X. Liao, K.R. Clemens, J. Cavanagh, L. Tennant and P.E. Wright (1994) J. Biomol. NMR 4, 433-454.

“1H, 15N, and 13C resonance assignments, secondary structure, and the conformation of substrate in the binary folate complex of Escherichia coli dihydrofolate reductase.”  C.J. Falzone, J. Cavanagh, M. Cowart, A.G. Palmer III, S.J. Benkovic, C.R. Matthews and P.E. Wright (1994) J. Biomol. NMR 4, 349-366.

1H resonance assignments and secondary structure of the carbon monoxide complex of soybean leghemoglobin determined by homonuclear 2D- and 3D-NMR spectroscopy.”  D. Morikis, C.A. Lepre and P.E. Wright (1994) Eur. J. Biochem. 219, 611-626.

“POU domains and homeodomains.”  P.E. Wright (1994) Curr.  Opin. Struct. Biol. 4, 22-27.

“Dynamics of a flexible loop in dihydrofolate reductase from Escherichia coli and its implication for catalysis.”  C.J. Falzone, P.E. Wright and S.J. Benkovic (1994) Biochemistry 33, 439-442.

1993

“Biophysical methods: Editorial overview.”  J.L. Smith and P.E. Wright (1993) Curr. Opin. Struct. Biol. 3, 723-724.

“NMR evidence for multiple conformations in a highly helical model peptide.”  G. Merutka, D. Morikis, R. Brüschweiler and P.E. Wright (1993) Biochemistry 32, 13089-13097.

“Characterization of a folding intermediate of apoplastocyanin trapped by proline isomerization.”  S. Koide, H.J. Dyson and P.E. Wright (1993) Biochemistry 32, 12299-12310.

Formation of a molten globule intermediate in the kinetic folding pathway of apomyoglobin.”  P.A. Jennings and P.E. Wright (1993) Science 262, 892-896.

Binding of a high-energy substrate conformer in antibody catalysis.”  A.P. Campbell, T.M. Tarasow, W. Massefski, P.E. Wright, and D. Hilvert (1993) Proc. Natl Acad. Sci. USA 90, 8663-8667.

“Electrostatic calculations of side-chain pKa values in myoglobin and comparison with NMR data for histidines.”  D.Bashford, D.A. Case, C. Dalvit, L. Tennant and P.E. Wright  (1993) Biochemistry 32, 8045-8056.

“Determination of local ligand conformations in slowly tumbling proteins by homonuclear 2D and 3D NMR:Application to heme propionates in leghemoglobin.”  D. Morikis, R. Brüschweiler and P.E. Wright (1993) J. Amer. Chem. Soc. 115, 6238-6246.

“Peptide models of protein folding initiation sites. 3. The G-H helical hairpin of myoglobin.”  H.-C. Shin, G. Merutka, J.P. Waltho, L.L. Tennant, H.J. Dyson and P.E. Wright (1993) Biochemistry 32, 6356-6364.

“Peptide models of protein folding initiation sites.  2. The G-H turn region of myoglobin acts as a helix stop signal.”  H.-C. Shin, G. Merutka, J.P. Waltho, P.E. Wright and H. J. Dyson (1993) Biochemistry 32, 6348-6355.

Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobin.”  J.P. Waltho, V.A.Feher, G. Merutka, H.J. Dyson and P.E. Wright (1993) Biochemistry 32, 6337-6347.

“Characterization of amino acid side chain dynamics in a zinc finger peptide using 13C NMR spectroscopy and time-resolved fluorescence spectroscopy.”  A.G. Palmer, III, R.A. Hochstrasser, D.P. Millar, M. Rance and P.E. Wright (1993)  J. Amer. Chem. Soc. 115, 6333-6345.

Structure of the retinoid X receptor a DNA-binding domain: A helix required for homodimeric DNA binding.”  M.S. Lee, S.A. Kliewer, J. Provencal, P.E. Wright and R.M. Evans (1993) Science 260, 1117-1121.

“Peptide conformation and protein folding.”  H.J. Dyson and P.E. Wright (1993) Curr. Opin. Struct. Biol. 3, 60-65.

The solution structure of the Oct-1 POU-specific domain reveals a striking similarity to the bacteriophage l repressor DNA-binding domain.”  N. Assa-Munt, R. Mortishire-Smith, R. Aurora, W.Herr and P.E. Wright (1993) Cell 73, 193‑205.

Molecular basis for specific recognition of both RNA and DNA by a zinc finger protein.”  K.R. Clemens, V. Wolf, S.J. McBryant, P. Zhang, X. Liao, P.E. Wright and J.M. Gottesfeld (1993) Science 260, 530-533.

Assignments of 1H, 15N and 13C resonances, identification of elements of secondary structure and determination of the global fold of the DNA binding domain of GAL4.”  M. Shirakawa, W.J. Fairbrother, Y. Serikawa, T. Ohkubo, Y. Kyogoku and P.E. Wright (1993) Biochemistry 32, 2144-2153.

“Mapping of the binding interfaces of the proteins of the bacterial phosphotransferase system, HPr and IIAglc.”  Y. Chen, J. Reizer, M.H. Saier, W.J. Fairbrother and P.E. Wright (1993) Biochemistry 32, 32-37.

Three-dimensional structures of the central regulatory proteins of the bacterial phosphotransferase system, HPr and enzyme IIAglc.”  Y. Chen, W.J. Fairbrother and P.E. Wright (1993) J. Cell. Biochem., 51, 75-82.

Comparison of backbone and tryptophan sidechain dynamics of reduced and oxidized E. coli thioredoxin using 15N NMR relaxation measurements.”  M.J. Stone, K. Chandrasekhar, A. Holmgren, P.E. Wright and H.J. Dyson (1993) Biochemistry 32, 426-435.

“Determination of high resolution NMR structures of proteins.”  D.A. Case and P.E. Wright (1993) In: “NMR of Proteins,” Eds. G.M. Clore and A.M. Gronenborn, MacMillan, pp. 53-91.

1992

Definition of the binding sites of individual zinc fingers in the TFIIIA-5S RNA gene complex.”  K.R. Clemens, X. Liao, V. Wolf, P.E. Wright and J.M. Gottesfeld (1992)  Proc. Natl Acad. Sci. USA 89, 10822-10826.

“Functional role of a mobile loop of Escherichia coli dihydrofolate reductase in transition state stabilization.”  L. Li, C.J. Falzone, P.E. Wright and S.J. Benkovic (1992) Biochemistry 31, 7826-7833.

The zinc finger motif:  Conservation of chemical shifts and correlation with structure.”  M.S.Lee, R.J. Mortishire-Smith, and P.E. Wright (1992) FEBS Lett. 309, 29-32.

“Conformation and dynamics of an Fab’-bound peptide by isotope-edited NMR spectroscopy.”  P. Tsang, M. Rance, T.M. Fieser, J.M. Ostresh, R.A. Houghten, R.A. Lerner and P.E. Wright (1992) Biochemistry 31, 3862-3871.

Assignment of the aliphatic 1H and 13C resonances of the Bacillus subtilis glucose permease IIA domain using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopy.”  W.J. Fairbrother, A.G. Palmer, III, M. Rance, J. Reizer, M.H. Saier, Jr. and P.E. Wright (1992) Biochemistry 31, 4413‑4425.

Backbone dynamics of the Bacillus subtilis glucose permease IIA domain determined from 15N NMR relaxation measurements.”  M.J. Stone, W.J. Fairbrother, A.G. Palmer III, J. Reizer, M.H. Saier Jr. and P.E. Wright (1992) Biochemistry 31, 4394-4406.

“Relationship between 1H and 13C NMR chemical shifts and the secondary and tertiary structure of a zinc finger peptide.”  M.S. Lee, A.G. Palmer III and P.E. Wright (1992) J. Biomol. NMR 2, 307-322.

Folding of peptide fragments comprising the complete sequence of proteins:Models for initiation of protein folding.  II. Plastocyanin.”  H.J. Dyson, J.R. Sayre, H-C. Shin, G. Merutka, R.A. Lerner and P.E. Wright (1992) J. Mol. Biol. 226, 819-835.

Folding of peptide fragments comprising the complete sequence of proteins:   Models for initiation of protein folding.  I. Myohemerythrin.”  H.J. Dyson, G. Merutka, J.P. Waltho, R.A. Lerner and P.E. Wright (1992) J. Mol. Biol. 226, 795‑817.

Structural determinants of Cys2 His2 zinc fingers.”  R.J. Mortishire-Smith, M.S. Lee, L. Bolinger and P.E. Wright (1992) FEBS Lett. 296, 11-15.

Low resolution solution structure of the Bacillus subtilis glucose permease IIA domain derived from heteronuclear three-dimensional NMR spectroscopy.”  W.J. Fairbrother, G.P. Gippert, J. Reizer, M.H. Saier  Jr. and P.E. Wright (1992) FEBS Lett. 296, 148-152.

“Improved resolution in three-dimensional constant-time triple resonance NMR spectroscopy of proteins.”  A.G. Palmer III, W.J. Fairbrother, J. Cavanagh, P.E. Wright and M. Rance (1992) J. Biomol. NMR 2, 103-108.

“Immunogenic peptides corresponding to the dominant antigenic region alanine-597 to cysteine-619 in the transmembrane protein of simian immunodeficiency virus have a propensity to fold in aqueous solution.”  H.J. Dyson, E. Norrby, K. Hoey, D.E. Parks, R.A. Lerner and P.E. Wright (1992) Biochemistry 31, 1458‑1463.

Specific interactions of the first three zinc fingers of TFIIIA with the internal control region of the Xenopus 5S RNA gene.”  X. Liao, K. Clemens, L. Tennant, P.E. Wright and J. Gottesfeld (1992) J. Mol. Biol. 223, 857-871.

“A comparison of the requirements for pre-formed secondary structure in proteins with different structures in the folded state.”  H.J. Dyson and P.E. Wright (1992) In: “Proceedings of Seventh Conversation in Biomolecular Stereodynamics.  Structure and Function, Volume 2:Proteins,” Eds. R.H. Sarma and M.H. Sarma, Adenine Press, Albany, NY, pp. 113-120.

“Suppression of the effects of cross-correlation between dipolar and anisotropic chemical shift relaxation mechanisms in the measurement of spin-spin relaxation rates.”  A.G. Palmer III, N.J. Skelton, W.J. Chazin, P.E. Wright and M. Rance (1992) Mol. Phys., 75, 699-711.

“Solution structures of DNA-binding domains of eukaryotic transcription factors.”  P.E. Wright (1992) In: “Transcriptional Regulation,” Eds. K. Yamamoto and S. McKnight, Cold Spring Harbor Laboratory Press,  pp. 579-597.

1991

High-resolution solution structure of reduced French bean plastocyanin and comparison with the crystal structure of poplar plastocyanin.”  J.M. Moore, C. Lepre, G.P. Gippert, W.J. Chazin, D.A. Case and P.E. Wright (1991) J. Mol. Biol. 221, 533-555.

“Measurement of relaxation rate constants for methyl groups by proton-detected heteronuclear NMR spectroscopy.”  A.G. Palmer III, P.E. Wright and M. Rance (1991) Chem. Phys. Lett. 185, 41-46.

Polypeptide backbone resonance assignments and secondary structure of Bacillus subtilis enzyme IIIglc determined by two-dimensional and three-dimensional heteronuclear NMR spectroscopy.”  W.J. Fairbrother, J. Cavanagh, H.J. Dyson, A.G. Palmer, S.L. Sutrina, J. Reizer, M.H. Saier, and P.E. Wright (1991) Biochemistry 30, 6896-6907.

“Intramolecular motions of a zinc finger DNA-binding domain from Xfin characterized by proton-detected natural abundance 13C heteronuclear NMR spectroscopy.”  A.G. Palmer III, M. Rance and P.E. Wright (1991) J. Amer. Chem. Soc. 113, 4371-4380.

“Sensitivity improvement in proton detected two-dimensional heteronuclear correlation NMR spectroscopy.”  A.G. Palmer III. J. Cavanagh, P.E. Wright and M. Rance (1991) J. Magn. Reson. 93, 151-170.

“Evidence for two interconverting protein isomers in the methotrexate complex of dihydrofolate reductase from Escherichia coli.”  C.J. Falzone, P.E. Wright and S.J. Benkovic (1991) Biochemistry 30, 2184-2191.

Mapping the anatomy of the immunodominant domain of the HIV GP41 transmembrane protein: Peptide conformation analysis using monoclonal antibodies and proton nuclear magnetic resonance spectroscopy.”  M.B.A. Oldstone, A. Tishon, H. Lewicki, H.J. Dyson, V.A. Feher, N. Assa-Munt and P.E. Wright (1991) J. Virol. 65, 1727-1734.

Kinetics and mechanism of reduction of Cu(II) and Fe (III) complexes by soybean leghemoglobin a.”  D.A. Bakan, P. Saltman, Y. Theriault and P.E. Wright (1991) Biochim. Biophys. Acta, 1079, 182-196.

Defining solution conformations of small linear peptides.”  H.J. Dyson and P.E. Wright (1991) Ann. Rev. Biophysics Biophys. Chem. 20, 519-538.

“The three-dimensional solution structure of human anaphylatoxin C3a.”  M.W. Kalnik, W.J. Chazin and P.E. Wright (1991) In: “Techniques in Protein Chemistry II,” Ed. J.J. Villafranca, Academic Press, San Diego, pp. 393-400.

“Isotope-edited nuclear magnetic resonance studies of Fab-peptide complexes.”  P. Tsang, M. Rance and P.E. Wright (1991) In: “Methods in Enzymology,” Vol. 203, 241-261.

“Sensitivity improvement in proton-detected two-dimensional heteronuclear relay spectroscopy.”  J. Cavanagh, A.G. Palmer III, P.E. Wright & M. Rance (1991) J. Magn. Reson. 91, 429-436.

Zinc is required for folding and binding of a single zinc finger to DNA.”  M.S. Lee, J.M. Gottesfeld and P.E. Wright (1991) FEBS Lett. 279, 289-294.

1990

The conformational restriction of synthetic vaccines for malaria.”  A.C. Satterthwait, L.-C. Chiang, T. Arrhenius, E. Cabezas, F. Zavala, H.J. Dyson, P.E. Wright and R.A. Lerner (1990) Bull. World Hlth Organiz. 68 (Suppl), 17‑25.

“Specific deuteration strategy for enhancing direct nuclear Overhauser effects in high molecular weight complexes.”  P. Tsang, P.E. Wright and M. Rance (1990) J. Amer. Chem. Soc. 112, 8183-8185.

“1H NMR assignments of the Escherichia coli dihydrofolate reductase complex with folate: Evidence for a unique conformation of bound folate.”  C.J. Falzone, S.J. Benkovic and P.E. Wright (1990) Biochemistry 29, 9667-9677.

Structural characterization of a partly folded apomyoglobin intermediate.”  F.M. Hughson, P.E. Wright and R.L. Baldwin (1990) Science 249, 1544-1548.

“Signal suppression in the frequency domain to remove undesirable resonances with dispersive lineshapes.”  P. Tsang, P.E. Wright and M. Rance (1990) J. Magn. Reson. 88, 210-215.

Conformational preferences of synthetic peptides derived from the immunogenic site of the circumsporozoite protein of Plasmodium falciparum by 1H NMR.”  H.J. Dyson, A.C. Satterthwait, R.A. Lerner and P.E. Wright (1990) Biochemistry 29, 7828-7837.

Antigen-antibody interactions: an NMR approach.”  P.E. Wright, H.J. Dyson, R.A. Lerner, L. Riechmann and P. Tsang.  (1990) Biochem. Pharmacol. 40, 83‑88.

“The H-helix of myoglobin as a potential independent protein folding domain.”  J.P. Waltho, V.A. Feher and P.E. Wright (1990), In: Current Research in Protein Chemistry:  Techniques, Structure and Function, The Protein Society, Ed. J.J. Villafranca, Academic Press, San Diego, 283-293.

Computational methods for determining protein structures from NMR data.”  G.P. Gippert, P.F. Yip, P.E. Wright and D.A. Case (1990) Biochem. Pharmacol. 40, 15-22.

“Proton Nuclear Magnetic Resonance assignments and solution structure of a synthetic zinc finger from Xfin.” M.S. Lee, G.P. Gippert, K.V. Soman, D.A. Case and P.E. Wright (1990), In: Proceedings of Sixth Conversation in Biomolecular Stereodynamics.  Structure and Methods: Volume 2, DNA-Protein Complexes and Proteins, Eds. R.H. Sarma and M.H. Sarma, Adenine Press, Albany, NY, 83-91.

Three-dimensional solution structure of the reduced form of Escherichia coli thioredoxin determined by NMR spectroscopy.”  H.J. Dyson, G.P. Gippert, D.A. Case, A. Holmgren and P.E. Wright (1990) Biochemistry 29, 4129-4136.

“Solution NMR studies of Fab’-peptide complexes.”  P. Tsang, T.M. Fieser, J.M. Ostresh, R.A. Houghten, R.A. Lerner and P.E. Wright (1990) In: Frontiers of NMR in Molecular Biology, UCLA Symposia on Molecular and Cellular Biology, New Series, Eds. D. Live, I. Armitage and D. Patel, Vol. 109, Alan R. Liss, Inc., New York, 63-73.

“Folding of peptide fragments of proteins in aqueous solution.”  P.E. Wright, H.J. Dyson, V.A. Feher, L. Tennant, J.P. Waltho, R.A. Lerner and D.A. Case (1990), In: Frontiers of NMR in Molecular Biology, UCLA Symposia on Molecular and Cellular Biology, New Series, Eds. D. Live, I. Armitage and D. Patel, Vol. 109, Alan R. Liss, Inc., New York, 1-13.

1989

“Folding of peptide fragments of proteins in water solution:  implications for initiation of protein folding.”  P.E. Wright, R.A. Lerner and H.J. Dyson (1989), In: Advances in Protein Design, Eds. H. Blocker, J. Collins, R.D. Schmid, D. Schomburg, VCH Publishers, 13-19.

Complete assignment of the 1H nuclear magnetic resonance spectrum of a synthetic zinc finger from Xfin.  Sequential resonance assignments and secondary structure.”  M.S. Lee, J. Cavanagh and P.E. Wright (1989) FEBS Lett. 254, 159‑164.

Three-dimensional solution structure of a single zinc finger DNA-binding domain.”  M.S. Lee, G.P. Gippert, K.V. Soman, D.A. Case and P.E. Wright (1989) Science 245, 635-637.

What can two-dimensional NMR tell us about proteins?”  P.E. Wright (1989) Trends Biochem. Sci. 14, 255-260.

Conformation of a T cell stimulating peptide in aqueous solution.”  J.P. Waltho, R.A. Lerner and P.E. Wright (1989) FEBS Lett. 250, 400-404.

“Assignment of the proton NMR spectrum of reduced and oxidized thioredoxin: sequence-specific assignments, secondary structure and global fold.”  H.J. Dyson, A. Holmgren and P.E. Wright (1989) Biochemistry 28, 7074-7087.

“Folding of peptide fragments of proteins in water solution.”  P.E. Wright, H.J. Dyson and R.A. Lerner (1989), In: Protein Folding.  Deciphering the Second Half of the Genetic Code, Eds. J.A. King and L.M. Gierasch, AAAS, 95-102.

1H NMR studies of the solution conformations of an analogue of the C-peptide of ribonuclease A.”  J.J. Osterhout, Jr., R.L. Baldwin, E.J. York, J.M. Stewart, H.J. Dyson and P.E. Wright (1989) Biochemistry 28, 7059-7064.

Chemical modification of bovine pancreatic trypsin inhibitor for single site coupling of immunogenic peptides for NMR conformational analysis.”  S. Ebina, R.A. Lerner and P.E. Wright (1989) J. Biol. Chem. 264, 7882-7888.

“Multiple Quantum NMR.”  M. Rance, W.J. Chazin, C. Dalvit and P.E. Wright (1989), In: “Methods in Enzymology,” Eds. N. Oppenheimer and T.L. James,  Vol. 176, 114-134.

1988

NMR studies of the conformations of leghemoglobins from soybean and lupin.”  S.S. Narula, C. Dalvit, C.A. Appleby and P.E. Wright (1988) Eur. J. Biochem. 178, 419-435.

Isotope-edited NMR studies of Fab-peptide complexes.”  P. Tsang, T.M. Fieser, R.A. Houghten, R.A. Lerner and P.E. Wright (1988) Pept. Res. 1, 87-92.

1H NMR studies of human C3a anaphylatoxin in solution: sequential resonance assignments, secondary structure and global fold.”  W.J. Chazin, T.E. Hugli and P.E. Wright (1988) Biochemistry 27, 9139-9148.

1H NMR studies of plastocyanin from Scenedesmus obliquus:  Complete sequence-specific assignment, secondary structure analysis and global fold.”  J.M. Moore, W.J. Chazin, R. Powls and P.E. Wright (1988) Biochemistry 27, 7806‑7816.

Conformation of peptide fragments of proteins in aqueous solution: implications for initiation of protein folding.”  P.E. Wright, H.J. Dyson and R.A. Lerner (1988) Biochemistry 27, 7167-7175.

Three-dimensional solution structure of plastocyanin from the green alga Scenedesmus obliquus.”  J.M. Moore, D.A. Case, W.J. Chazin, G.P. Gippert, T.F. Havel, R. Powls and P.E. Wright (1988) Science 240, 314-317.

Structural differences between oxidized and reduced thioredoxin monitored by two-dimensional 1H NMR spectroscopy.”  H.J. Dyson, A. Holmgren and P.E. Wright (1988) FEBS Lett. 228, 254-258.

“Complete assignment of the 1H NMR spectrum of French bean plastocyanin: sequential resonance assignments, secondary structure and global fold.”  W.J. Chazin and P.E. Wright (1988) J. Mol. Biol. 202, 623-636.

Complete assignment of the 1H NMR spectrum of French bean plastocyanin: application of an integrated approach to spin system identification in proteins.”  W.J. Chazin, M. Rance and P.E. Wright (1988) J. Mol. Biol. 202, 603-622.

“Kinetic studies on 1:1 electron transfer reactions involving blue copper proteins. 16. The reactivity of plastocyanin from the green alga Scenedesmus obliquus with inorganic redox partners and related NMR studies.”  J. McGinnis, J.D. Sinclair‑Day, A.G. Sykes, R. Powls, J. Moore and P.E. Wright (1988) Inorg. Chem. 27, 2306-2312.

[On the basis of immunogenic peptides for induction of protein-reactive anti-peptide antibodies in view of peptide conformation] [Article in Japanese]  S. Ebina and P.E. Wright (1988) Seikagaku 60(5), 348-352

The physical basis induction of protein-reactive anti-peptide antibodies.”  H.J. Dyson, R.A. Lerner and P.E. Wright (1988) Ann. Rev. Biophysics Biophys. Chem. 17, 305-324.

Folding of immunogenic peptide fragments of proteins in water solution.  II. The nascent helix.”  H.J. Dyson, M. Rance, R.A. Houghten, P.E. Wright and R.A. Lerner (1988) J. Mol. Biol. 201, 201-217.

Folding of immunogenic peptide fragments of proteins in water solution.  I. Sequence requirements for the formation of a reverse turn.”  H.J. Dyson, M. Rance, R.A. Houghten, R.A. Lerner and P.E. Wright (1988) J. Mol. Biol. 201, 161-200.

1987

Electron transfer from cytochrome b5 to iron and copper complexes.”  L.S. Reid, H.B. Gray, C. Dalvit, P.E. Wright and P. Saltman (1987) Biochemistry 26, 7102‑7107.

Complete assignment of lysine resonances in 1H NMR spectra of proteins as probes of surface structure and dynamics.”  W.J. Chazin, M. Rance and P.E. Wright (1987) FEBS Lett. 222, 109-114.

“Kinetic studies on 1:1 electron-transfer reactions involving blue copper proteins.  Part 15. The reactivity of Anabaena variabilis plastocyanin with inorganic complexes and related NMR studies.”  M.P. Jackman, J.D. Sinclair-Day, M.J. Sisley, A.G. Sykes, L.A. Denys and P.E. Wright (1987) J. Amer. Chem. Soc. 109, 6443-6449.

Structural consequences of heme isomerism in monomeric hemoglobins from Glycera dibranchiata.”  R.M. Cooke and P.E. Wright (1987) Eur. J. Biochem. 166, 409-414.

NMR studies of the heme pocket conformations of monomeric hemoglobins from Glycera dibranchiata.  Implications for ligand binding.”  R.M. Cooke, C. Dalvit, S.S. Narula and P.E. Wright (1987) Eur. J. Biochem. 166, 399-408.

“Identification of folded structures in immunogenic peptides by 2D NMR spectroscopy.”  P.E. Wright, H.J. Dyson, M. Rance, R.A. Houghten and R.A. Lerner (1987), In: Protides of the Biological Fluids, Ed. H. Peeters, Vol. 35, Pergamon Press, Oxford, pp. 477-480.

A modified approach to identification of 1H spin systems in proteins.”  W.J. Chazin and P.E. Wright (1987) Biopolymers 26, 973-977.

1H resonances of proximal histidine in CO complexes of hemoglobins provide a sensitive probe of coordination geometry.”  C. Dalvit, L. Tennant and P.E. Wright (1987) FEBS Lett. 213, 289-292.

“Site-selective observation of nuclear Overhauser effects in proteins via isotopic labeling.”  M. Rance, P.E. Wright, B.A. Messerle and L.D. Field (1987) J. Am. Chem. Soc. 109, 1591-1593.

Assignment of resonances in the 1H NMR spectrum of the carbon monoxide complex of human hemoglobin a-chains.”  C. Dalvit and P.E. Wright (1987) J. Mol. Biol. 194, 329-339.

Assignment of resonances in the 1H NMR spectrum of the carbon monoxide complex of sperm whale myoglobin by phase sensitive two-dimensional techniques.”  C.  Dalvit and P.E. Wright (1987) J. Mol. Biol. 194, 313-327.

“Detection of long-range couplings in proteins via double quantum spectroscopy: Connection of alphatic and imidazole resonances of histidine residues.”  C. Dalvit, P.E. Wright and M. Rance (1987) J. Magn. Reson. 71, 539-543.

Kinetic and mechanisms of the oxidation of myoglobin by Fe(III) and Cu(II) complexes.”  K. Hegetschweiler, P. Saltman, C. Dalvit and P.E. Wright (1987) Biochim. Biophys. Acta 912, 384-397.

“The order-disorder paradox in antigen-antibody union: anti-peptide antibodies as a probe for structured regions of small peptides.”  H.J. Dyson, M. Rance, R.A. Houghten, P.E. Wright and R.A. Lerner (1987), In: “Biological Organization: Macromolecular Interactions at High Resolution,” Eds. R.M. Burnett and H.J. Vogel, Academic Press, pp. 227-234.

1986

1H NMR studies of heme pocket conformation in zinc-substituted leghemoglobin, a diamagnetic analogue of deoxyleghemoglobin.”  C. Dalvit, L. Tennant and P.E. Wright (1986) J. Inorg. Biochem. 28, 303-309.

“Differentiation of direct and remote connectivities in phase sensitive double quantum spectra of proteins by variation of the multiple quantum excitation period.”  C. Dalvit, M. Rance and P.E. Wright (1986) J. Magn. Reson. 69, 356‑361.

“Proton NMR studies of plastocyanin: Assignment of aromatic and methyl group resonances from 2D spectra.”  G. King and P.E. Wright (1986) Biochemistry 25, 2364-2374.

“Selection rule violations in multiple quantum NMR spectroscopy.”  M. Rance and P.E. Wright (1986) Chem. Phys. Lett. 124, 572-575.

Assignment of methylene proton resonances in NMR spectra of of embryonic and transformed cells to plasma membrane triglyceride.”  G.L. May, L.C. Wright, K.T. Holmes, P.G. Williams, I.C.P. Smith, P.E. Wright, R.M. Fox and C.E. Mountford (1986) J. Biol. Chem. 261, 3048-3053.

“1H NMR studies of high spin complexes of soybean leghemoglobin.  Interactions between the distal histidine and acetate, formate and fluoride ligands.”  J. Trewhella, C.A. Appleby and P.E. Wright (1986) Aust. J. Chem. 39, 317-324.

“Analysis of 1H NMR spectra of proteins using multiple quantum coherence.”  M. Rance and P.E. Wright (1986) J. Magn. Res. 66, 372-378.

“Selection by site-directed antibodies of small regions of peptides which are ordered in water.”  H.J. Dyson, K.J. Cross, J. Ostresh, R.A. Houghten, I.A. Wilson, P.E. Wright and R.A. Lerner (1986), In: Synthetic Peptides as Antigens, Ciba Foundation Symposium 119, John Wiley & Sons, Chichester, pp. 58-75.

1985

“Heme orientation in the major monomeric hemoglobins of Glycera dibranchiata.”  R.M. Cooke and P.E. Wright (1985) Biochim. Biophys. Acta 832, 357-372.

“Differences in amino acid composition and heme electronic structure of the multiple monomeric hemoglobin components of Glycera dibranchiata.”  R.M. Cooke and P.E. Wright (1985) Biochim. Biophys. Acta 832, 357-364.

“Antipeptide antibodies and the disorder-order phenomenon.”  P.E. Wright, H.J. Dyson, M. Rance, J. Ostresh, R.A. Houghten, I.A. Wilson and R.A. Lerner (1986), In: New Approaches to Immunization, Eds. R.M. Chanock, F. Brown and R.A. Lerner, Cold Spring Harbor Press, New York, 15-19.

The immunodominant site of a synthetic immunogen has a conformational preference in water for a type II reverse turn.”  H.J. Dyson, K.J. Cross, R.A. Houghten, I.A. Wilson, P.E. Wright and R.A. Lerner (1985) Nature 318, 480-483.

Assignment of heme and distal amino acid resonances in the 1H NMR spectra of the carbon monoxide and oxygen complexes of sperm whale myoglobin.”  B.C. Mabbutt and P.E. Wright (1985) Biochim. Biophys. Acta 832, 175-185.

Simplification of 1H NMR spectra of proteins by one-dimensional multiple quantum filtration.”  M. Rance, C. Dalvit and P.E. Wright (1985) Biochem. Biophys. Res. Commun. 131, 1094-1102.

“Completely synthetic vaccine effective against heterologous enterotoxigenic Escherichia coli.”  R.A.van Houghten, R.A. Lerner, S.R. Hoffman, P.A. Worrell, P.E. Wright and F.A. Klipstein (1985), In: Vaccines ’85.  Molecular and Chemical Basis of Resistance to Parasitic, Bacterial and Viral Diseases, Eds. R.A. Lerner, R.M. Chanock and F. Brown, Cold Spring Harbor Laboratory, New York, 91-94.

Conformational disorder of the distal leucine in monomeric Glycera hemoglobins and implications for oxygen binding.”  R.M. Cooke and P.E. Wright (1985) FEBS. Lett. 187, 219-223.

“Acid dissociation constants for plastocyanin in the Cu(I) state.”  J.D. Sinclair‑Day, M.J. Sisley, A.G. Sykes, G.C. King and P.E. Wright (1985) Chem. Comm. 505-507.

“Calibration of ring current models for the heme ring.”  K.J. Cross and P.E. Wright (1985) J. Magn. Res. 64, 220-231.

“NMR studies of the structure and dynamics of monomeric hemoglobins and myoglobins.”  P.E. Wright, R.M. Cooke, K.J. Cross, B.C. Mabbutt, B.A. Messerle and J.E. Wellington (1985) In: Magnetic Resonance in Biology and Medicine, Eds. G. Govil, C.L. Khetrapal and A. Saran, Tata-McGraw-Hill, New Delhi, 131-150.

1H NMR studies of the conformation of eosinophil chemotactic tetra-peptides and analogues in DMSO.”  G.R. Beilharz, J.A. Smith, K.F. Austen and P.E. Wright (1985) Int. J. Peptide Protein Chem. 25, 337-346.

NMR and kinetic characterization of the interaction between French bean plastocyanin and horse cytochrome c.”  G.C. King, R.A. Binstead and P.E. Wright (1985) Biochim. Biophys. Acta 806, 262-271.

1984

Assignment of acyl chain resonances from membranes of mammalian cells by two dimensional methods.”  K.J. Cross, K.T. Holmes, C.E. Mountford and P.E. Wright (1984) Biochemistry 23, 5895-5897.

“NMR studies of myelin basic protein – XI.  Conformation of a nona-peptide from a segment encephalitogenic in Rhesus monkey.”  G.L. Mendz, W.J. Moore, G. King and P.E. Wright (1984) Int. J. Peptide Protein Chem. 24, 208-217.

“Unequivocal proof of chlorophyll formation by the C5 pathway and tenative evidence for Shemin pathway activity in greening leaves.  Is mitochondrial haem formed by the Shemin pathway in leaf cells?”  R.J. Porra, O. Klein and P.E. Wright (1984), In: “Advances in Photosynthesis Research,” Eds. C. Sybesma, M. Nijhoff, and W. Junk, Vol. IV, 6.725-6.728.

“An examination of the basic blue copper protein from cucumber peelings by 1H NMR.”  G. King, T.A. Andary, H.C. Freeman, L. Gavrilovic and P.E. Wright (1984) FEBS Lett. 166, 288-292.

1983

The proof by 13C NMR spectroscopy of the predominance of the C5 pathway over the Shemin pathway in chlorophyll biosynthesis in higher plants and of the formation of the methyl ester group of chlorophyll from glycine.”  R.J. Porra, O. Klein and P.E. Wright (1983) Eur. J. Biochem. 130, 509-516.

“Applications of two-dimensional relayed coherence transfer experiments to 1H NMR studies of macromolecules.”  G. King and P.E. Wright (1983) J. Mag. Res. 54, 328-332.

NMR studies of oxyleghemoglobin.  Assignment of distal histidine proton resonances and evidence for pH-dependent changes in conformation.”  B.C. Mabbutt, C.A. Appleby and P.E. Wright (1983) Biochim. Biophys. Acta 749, 281‑288.

“A proton NMR study of the conformation of Trp-Gly-Ala-Glu in dimethylsulphoxide.”  G.R. Beilharz, P. Mack, A.V. Robertson and P.E. Wright (1983) Aust. J. Chem. 36, 751-758.

“Assignment of heme and distal amino acid proton resonances in the NMR spectra of the oxygen and carbonmonoxide complexes of soybean leghemoglobin.”  B.C. Mabbutt and P.E. Wright (1983) Biochim. Biophys. Acta 744, 281-290.

Leghemoglobin.  Kinetic, NMR and optical studies of pH dependence of oxygen and carbon monoxide binding.”  C.A. Appleby, J.H. Bradbury, R.J. Morris, B.A. Wittenberg, J.B. Wittenberg and P.E. Wright (1983) J. Biol. Chem. 258, 2254‑2259.

“1H NMR studies of complexes of ferric leghemoglobin with substituted pyridines and nicotinic acids.”  B.C. Mabbutt and P.E. Wright (1983) J. Inorg. Biochem. 18, 123-132.

1982

“13C NMR studies of chlorophyll biosynthesis in higher plants: an unequivocal proof of the participation of the C5 pathway and evidence of a new route for the incorporation of glycine.”  R.J. Porra, O. Klein and P.E. Wright (1982) Biochem. Internat. 5, 345-350.

A two-dimensional NMR method for assignment of imidazole ring proton resonances of histidine residues in proteins.”  G. King and P.E. Wright (1982) Biochem. Biophys. Res. Commun. 106, 559-565.

“A comment on resonance Raman spectroscopic investigations of axial ligation of the heme iron atom in soybean leghemoglobin a.”  R.S. Armstrong, M.J. Irwin, J.E. Wellington and P.E. Wright (1982) Acta Chem. Scand. 36B, 263-265.

“The mobile distal histidine of leghemoglobin: Does it control oxygen binding kinetics?”  C.A. Appleby, W.E. Blumberg, J.H. Bradbury, W.H. Fuchsman, J. Peisach, B.A. Wittenberg, J.B. Wittenberg and P.E. Wright (1982) In: Interactions Between Iron and Proteins in Oxygen and Electron Transport, Ed. C. Ho, Elsevier, 435-441.

“Differences in the heme environment of soybean leghemoglobin components shown by 1H NMR spectroscopy.”  C.A. Appleby, J. Trewhella and P.E. Wright (1982) Biochim. Biophys. Acta 700, 171-177.

“Soret excited resonance Raman spectrum of carbonmonoxleghemoglobin: assignment of uFe-CO.”  R.S. Armstrong, M.J. Irwin and P.E. Wright (1982) J. Amer. Chem. Soc. 104, 626-627.

1981

“Molecular basis for the pH-dependent binding of O2 to soybean leghemoglobin.”  P.E. Wright and C.A. Appleby (1981) Proc. Aust. Biochem. 14, 33.

“Resonance Raman studies of soybean leghemoglobin and myoglobin.  Origin of the differences in O2 dissociation rate constants.”  M.J. Irwin, R.S. Armstrong and P.E. Wright (1981) FEBS Lett. 133, 239-243.

“Heme pocket structure, conformational mobility and heme accessibility of soybean leghemoglobin.”  P.E. Wright and C.A. Appleby, 1981 In: Current Perspectives in Nitrogen Fixation, Eds. A.H. Gibson and W.E. Newton, Australian Academy of Science, 365.

Measurement of heme accessibility in soybean ferric leghemoglobin a and its complexes by proton magnetic relaxation.”  D.L. Ollis, P.E. Wright, J.M. Pope and C.A. Appleby (1981) Biochemistry 20, 587-594.

1980

Resonance Raman evidence for constrained heme structure in soybean leghemoglobin and its derivatives.”  R.A. Armstrong, M.J. Irwin and P.E. Wright (1980) Biochem. Biophys. Res. Commun. 95, 682-689.

“1H NMR studies of ferric soybean leghemoglobin.  Assignment of hyperfine shifted resonances of complexes with cyanide, nictinate, pyridine and azide.”  J. Trewella and P.E. Wright (1980) Biochim. Biophys. Acta 625, 202-220.

“1H NMR and EPR studies on skeletal muscle actin indicate that the metal and nucleotide binding sites are separate.”  J.A. Barden, R. Cooke, P.E. Wright and C.G. dos Remedios (1980) Biochemistry 19, 5912-5916.

NMR study of the interactions of plastocyanin with chromium (III) analogues of inorganic electron transfer reagents.”  D.J. Cookson, M.T. Hayes and P.E. Wright (1980) Biochim. Biophys. Acta. 591, 162-176.

“Electron transfer reagent binding sites on plastocyanin.”  D.J. Cookson, M.T. Hayes and P.E. Wright (1980) Nature 283, 682-683.

1979

“Conformation and dynamics of biological macromolecules in solution.”  P.E. Wright (1979) Proc. Aust. Soc. Biophysics 3, 1S-5S.

“Molecular basis for proton-dependent anion binding by soybean leghemoglobin a.”  J. Trewhella, P.E. Wright and C.A. Appleby (1979) Nature 280, 87-88.

“Spin state equilibria in soybean ferric leghemoglobin and its complexes with formate and acetate.”  J. Trewhella, P.E. Wright and C.A. Appleby (1979) Biochem. Biophys. Res. Commun. 88, 713-721.

1978

“The character of stored molecules in chromaffin granules of the adrenal medulla: a nuclear magnetic resonance study.”  A.J. Daniels, R.J.P. Williams and P.E. Wright (1978) Neurosc. 3, 573-585.

“High resolution proton magnetic resonance studies of plastocyanin.”  H.C. Freeman, V.A. Norris, J.A.M. Ramshaw and P.E. Wright (1978) FEBS Lett. 86, 131-135.

1977

“High resolution proton magnetic resonance studies of plastocyanin.”  H.C. Freeman, V.A. Norris, J.A.M. Ramshaw, and P.E. Wright (1977) In: Proceedings of the Fourth International Congress of Photosynthesis, 805-809.

The storage of small molecules in the octopus salivary gland:  nuclear magnetic resonance study.”  A. Daniels, J. Krebs, P.E. Wright and R.J.P. Williams (1977) Biochem. Soc. Trans. 5, 1149-1151.

“The proton NMR spectra of whole organs.”  A. Daniels, J. Krebs, B.A. Levine, P.E. Wright and R.J.P. Williams,  (1977) In: NMR in Biology, Eds. R.A. Dwek, I.D. Campbell, R.E. Richards and R.J.P. Williams, Academic Press, 277-287.

“Oxidation and reduction properties of cytochromes and peroxidases.”  R.J.P. Williams, G.R. Moore and P.E. Wright, (1977) In: Biological Aspects of Inorganic Chemistry., Eds. A.W. Addison, W.R. Cullen, D. Dolphin and B.R. James, Wiley, New York, 369-401.

“High resolution NMR studies of soybean leghemoglobin a.”  P.E. Wright and C.A. Appleby (1977) FEBS Lett. 78, 61-66.

1976

“Nuclear magnetic resonance studies of the adrenal gland and some other organs.”  A. Daniels, R.J.P. Williams and P.E. Wright (1976) Nature 261, 321-322.

A study of redox reactions of biological importance between Fe (III) complexes and aromatic moieties.”  P.S. Burns, J.F. Harrod, R.J.P. Williams and P.E. Wright (1976) Biochim. Biophys. Acta 428, 261-268.

1975

Pulse methods for the simplification of protein NMR spectra.”  I.D. Campbell, C.M. Dobson, R.J.P. Williams and P.E. Wright (1975) FEBS Lett. 57, 96-99.

Proton magnetic resonance studies of peroxidases from turnip and horseradish.”  R.J.P. Williams, P.E. Wright, G. Mazza and J.R. Ricard (1975) Biochim. Biophys. Acta 412, 127-147.

“Conformational studies of peroxidase-substrate complexes.  Structure of the indolepropionic acid-horseradish peroxidase complex.”  P.S. Burns, R.J.P. Williams and P.E. Wright (1975) J.C.S. Chem. Commun., 795-796.

“Assignment of NMR spectrum of iron (III) protoporphyrin (IX) dicyanide using paramagnetic shift and broadening probes.”  J.G. Brassington, R.J.P. Williams and P.E. Wright (1975) J.C.S. Chem. Commun., 338-340.

“Electronic transitions in salicylaldimine complexes.”  A.C. Braithwaite, P.E. Wright and T.N. Waters (1975) J. Inorg. Nucl. Chem. 37, 1669-1674.

“E.S.R. and optical spectral properties of copper (II) complexes with Schiff base ligands derived from o-amino-benzaldehyde.”  G.A. Bowmaker, T.N. Waters and P.E. Wright (1975) J. Chem. Soc. Dalton, 867-870.

1974

“Outline structure of cytochrome c3 and consideration of its properties.”  C.M. Dobson, N.J. Hoyle, C.F. Geraldes, M. Bruschi, J. LeGall, P.E. Wright and R.J.P. Williams (1974) Nature 249, 425-429.

1973

“Conformational influences in copper co-ordination compounds.  Part V.  Crystal and molecular structure of [1,2-bis(2-aminobenzylidene)-amino)propanato(2-)] copper (II).”  D. Hall, T.N. Waters and P.E. Wright (1973) J. Chem. Soc. Dalton, 1508-1512.

1971

“Electronic absorption band assignments for copper (II) salicylaldimine complexes.”  T.N. Waters and P.E. Wright (1971) J. Inorg. Nucl. Chem. 33, 359‑363.