1. Characteristics of a Bacillus subtilis W23 mutant temperature sensitive for chromosome replication. P. Upcroft, H.J. Dyson, & R.G. Wake
(1975) J. Bacteriol. 121, 121-127.
2. Spin state and unfolding equilibria of
ferricytochrome c in acidic solutions.
H.J. Dyson & J.K. Beattie (1982) J.
Biol. Chem. 257, 2267-2273.
3. 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, & R.A. Lerner (1985) Nature 318, 480-483.
4. Antipeptide antibodies and the disorder-order
phenomenon. P.E. Wright, H.J. Dyson, M.
Rance, J. Ostresh, R.A. Houghten, I.A. Wilson, & R.A. Lerner (1985) In: Modern Approaches to Vaccines (R.A. Lerner, R.M. Chanock, & F. Brown
Eds.)
5. 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, & R.A. Lerner (1986) In: Synthetic Peptides as Antigens, Ciba
Foundation Symposium 119 (R. Porter
& J. Whelan Eds.) John Wiley & Sons,
6. 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, & R.A. Lerner (1987) In: Biological Organization: Macromolecular
Interactions at High Resolution (R.M.
Burnett & H.J. Vogel Eds.) Academic Press Inc.,
7. Identification of folded structures in
immunogenic peptides by 2D NMR. P.E. Wright,
H.J. Dyson, M. Rance, R.A. Houghten, & R.A. Lerner (1987) In: Protides of the Biological Fluids, 35th
Colloquium (H. Peeters Ed.) Pergamon, pp
477-480.
8. The physical basis for induction of
protein-reactive antipeptide antibodies.
H.J. Dyson, R.A. Lerner, & P.E. Wright (1988) Ann. Rev. Biophys. Biophys. Chem. 17, 305-324.
9. 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, & P.E. Wright (1988) J. Mol. Biol. 201,
161-200.
10. 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, & R.A. Lerner (1988) J. Mol. Biol. 201,
201-217.
11. Structural
differences between oxidized and reduced thioredoxin monitored by
two-dimensional 1H NMR spectroscopy.
H.J. Dyson, A. Holmgren, & P.E. Wright (1988) FEBS Lett. 228, 254-258.
12. Conformation of
peptide fragments of proteins in aqueous solution: implications for initiation
of protein folding. P.E. Wright, H.J.
Dyson, & R.A. Lerner (1988) Biochemistry
27, 7167-7175.
13. Assignment of the
proton NMR spectrum of reduced and oxidized thioredoxin: sequence-specific
assignments, secondary structure and global fold. H.J. Dyson, A. Holmgren, & P.E. Wright
(1989) Biochemistry 28, 7074-7087.
14.1H 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, & P.E. Wright (1989) Biochemistry 28,
7059-7064.
15. Folding of
peptide fragments of proteins in water solution: implications for initiation of
protein folding. P.E. Wright, R.A.
Lerner, & H.J. Dyson (1989) In: Advances
in Protein Design (H. Blöcker, J.
Collins, R.D. Schmid, & D. Schomburg Eds.) VCH Publishing, pp 13-19.
16. Folding of
peptide fragments of proteins in aqueous solution. P.E. Wright, H.J. Dyson, V.A. Feher, L.L.
Tennant, J.P. Waltho, R.A. Lerner, & D.A. Case (1990) In: Frontiers of NMR in Molecular Biology,
UCLA Symposia in Molecular and Cellular Biology. New Series vol.109 (D. Live, I. Armitage, & D. Patel Eds.)
Alan R. Liss, Inc.,
17. Folding of
peptide fragments of proteins in water solution. P.E. Wright, H.J. Dyson, J.P. Waltho, &
R.A. Lerner (1990) In: Protein
Folding (L.M. Gierasch & J. King Eds.)
AAAS, Washington. pp 95-102.
18. Three-dimensional
solution structure of the reduced form of Escherichia
coli thioredoxin determined by nuclear magnetic resonance
spectroscopy. H.J. Dyson, G.P. Gippert,
D.A. Case, A. Holmgren, & P.E. Wright (1990) Biochemistry 29,
4129-4136.
19. Antigen-antibody
interactions: an NMR approach. P.E.
Wright, H.J. Dyson, R.A. Lerner, L. Riechmann, & P. Tsang (1990) Biochem. Pharm. 40, 83-88.
20. Conformational
preferences of synthetic peptides derived from the immunodominant site of the
circumsporozoite protein of Plasmodium
falciparum by 1H NMR. H.J.
Dyson, A.C. Satterthwait, R.A. Lerner, & P.E. Wright (1990) Biochemistry 29, 7828-7837.
21. 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 (1990) Bull. WHO 68, 17-25.
22. Defining solution
conformations of small linear peptides.
H.J. Dyson & P.E. Wright (1991) Ann.
Rev. Biophys. Biophys. Chem. 20,
519-538.
23. Active
conformation of an insect neuropeptide family.
R.J. Nachman, V.A. Roberts, H.J. Dyson, G.M. Holman, & J.A. Tainer
(1991) Proc. Natl. Acad. Sci. USA 88, 4518-4522.
24. Proton-transfer
effects in the active-site region of Escherichia
coli thioredoxin using two-dimensional 1H NMR. H.J. Dyson, L.L. Tennant, & A. Holmgren
(1991) Biochemistry 30, 4262-4268.
25. Mapping the
anatomy of the immunodominant domain of the human immunodeficiency virus 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, & P.E. Wright (1991) J. Virol. 65, 1727-1734.
26. Assignment of the
15N NMR
spectrum of reduced and oxidized Escherichia
coli thioredoxin. K. Chandrasekhar, G. Krause, A. Holmgren,
& H.J. Dyson (1991) FEBS Lett. 284, 178-183.
27. 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,III, S.L. Sutrina, J. Reizer, M.H. Saier,Jr, & P.E. Wright
(1991) Biochemistry 30, 6896-6907.
28. Solution
conformational preferences of immunogenic peptides derived from the principal
neutralizing determinant of the HIV-1 envelope glycoprotein gp120. K. Chandrasekhar, A.T. Profy, & H.J.
Dyson (1991) Biochemistry 30, 9187-9194.
29. Immunogenic
peptides corresponding to the dominant antigenic region Ala597 to Cys619 in the
transmembrane protein of simian immunodeficiency virus have a high folding
propensity. H.J. Dyson, E. Norrby, K.
Hoey, D.E. Parks, R.A. Lerner, & P.E. Wright (1992) Biochemistry 31,
1458-1463.
30. A comparison of
the requirements for pre-formed secondary structure in proteins with different
structures in the folded state. H.J.
Dyson & P.E. Wright (1992) Structure
and Function 2, 113-120.
31. 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, & P.E. Wright (1992) J. Mol.
Biol. 226, 795-817.
32. Folding of
peptide fragments comprising the complete sequence of proteins: models for the
initiation of protein folding II Plastocyanin.
H.J. Dyson, J.R. Sayre, G. Merutka, H.-C. Shin, R.A. Lerner, & P.E.
Wright (1992) J. Mol. Biol. 226, 819-835.
33. Peptide
conformation and protein folding. H.J.
Dyson & P.E. Wright (1993) Curr.
Opin. Struct. Biol. 3, 60-65.
34. Comparison of backbone
and tryptophan side-chain dynamics of reduced and oxidized Escherichia coli thioredoxin
using 15N NMR relaxation measurements. M.J. Stone, K. Chandrasekhar, A. Holmgren,
P.E. Wright, & H.J. Dyson (1993) Biochemistry
32, 426-435.
35. 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, & P.E. Wright (1993) Biochemistry 32,
6337-6347.
36. 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, & H.J. Dyson (1993) Biochemistry
32, 6348-6355.
37. 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, & P.E. Wright
(1993) Biochemistry 32, 6356-6364.
38. Characterization
of a folding intermediate of apoplastocyanin trapped by proline
isomerization. S. Koide, H.J. Dyson,
& P.E. Wright (1993) Biochemistry
32, 12299-12310.
39. Protein structure
calculation using NMR restraints. H.J.
Dyson & P.E. Wright (1994) In:
Two-Dimensional NMR Spectrscopy: Applications for Chemists and Biochemists (W.R. Croasmun & R. Carlson Eds.) VCH
Publishers, Inc.,
40. Peptide structure
in solution. H.J. Dyson (1994) In: Synthetic Vaccines (B.H. Nicholson Ed.) Blackwell Scientific
Publications Ltd,
41. Characterization
by 1H NMR of a C32S,C35S double mutant of Escherichia coli thioredoxin confirms its resemblance to the
reduced wild-type protein. H.J. Dyson,
M.-F. Jeng, P. Model, & A. Holmgren (1994) FEBS Lett. 339, 11-17.
42. Effect of
disulfide bridge formation on the NMR spectrum of a protein: studies on
oxidized and reduced Escherichia coli
thioredoxin. K. Chandrasekhar, A.P.
Campbell, M.-F. Jeng, A. Holmgren, & H.J. Dyson (1994) J. Biomol. NMR 4,
411-432.
43. Use of chemical
shifts and coupling constants in NMR structural studies on peptides and
proteins. D.A. Case, H.J. Dyson, &
P.E. Wright (1994) Methods Enzymol. 239, 392-416.
44. Detecting nascent
structures in solution using NMR. H.J.
Dyson, J. Yao, & P.E. Wright (1994)
In: Peptides: Chemistry, Structure and Biology (R.S. Hodges & J.A. Smith Eds.) ESCOM,
45. Binding of hapten
to a single-chain catalytic antibody demonstrated by ion spray mass
spectrometry. G. Siuzdak, J.F. Krebs,
S.J. Benkovic, & H.J. Dyson (1994) J.
Am. Chem. Soc. 116, 7937-7938.
46. 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, & H.J. Dyson
(1994) Structure 2, 853-868.
47. Stabilization of
a Type VI turn in a family of linear peptides in water solution. J. Yao, V.A. Feher, B.F. Espejo, M.T.
Reymond, P.E. Wright, & H.J. Dyson (1994) J. Mol. Biol. 243,
736-753.
48. 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, & P.E. Wright (1994) J. Mol. Biol. 243, 754-766.
49. Nuclear magnetic
resonance 15N and 1H resonance assignments and global
fold of rusticyanin: Insights into the ligation and acid stability of the blue
copper site. A.H. Hunt, A. Toy-Palmer,
N. Assa-Munt, J. Cavanagh, R.C. Blake,II, & H.J. Dyson (1994) J. Mol. Biol. 244, 370-384.
50. The folding
pathway of apomyoglobin. P.A. Jennings,
H.J. Dyson, & P.E. Wright (1994) In:
Statistical Mechanics, Protein Structure and Protein Substrate Interactions (S. Doniach Ed.) Plenum Press,
51. Analysis of peptide
and protein structure. H.J. Dyson
(1994) In: Immunological recognition of
peptides in medicine and biology (
52. Differential
hydration of side chain protons in a short peptide in a highly populated Type
VI turn conformation. J. Yao, R.
Brüschweiler, H.J. Dyson, & P.E. Wright (1994) J. Am. Chem. Soc. 116,
12051-12052.
53. Antigenic
peptides. H.J. Dyson & P.E. Wright
(1995) FASEB J. 9, 37-42.
54. Comparison of the
hydrogen exchange behavior of reduced and oxidized Escherichia coli thioredoxin.
M.-F. Jeng & H.J. Dyson (1995) Biochemistry
34, 611-619.
55. Detection of a
covalent intermediate in the reaction pathway of a catalytic antibody using
electrospray mass spectrometry. J.F.
Krebs, G. Siuzdak, H.J. Dyson, J.D. Stewart, & S.J. Benkovic (1995) Biochemistry 34, 720-723.
56. Peptide proton
random coil chemical shifts obtained as a function of temperature and
trifluoroethanol concentration. G.
Merutka, H.J. Dyson, & P.E. Wright (1995) J. Biomol. NMR 5, 14-24.
57. NMR of
thioredoxin and glutaredoxin. H.J. Dyson
(1995) Methods Enzymol. 252, 293-306.
58. Gene synthesis,
high-level expression and mutagenesis of Thiobacillus
ferrooxidans rusticyanin. His85 is a
ligand to the blue copper center. D.R.
Casimiro, A. Toy-Palmer, R.C. Blake,II, & H.J. Dyson (1995) Biochemistry 34,
6640-6648.
59. Complete 13C
resonance assignments and coupling constants for recombinant rusticyanin:
Prediction of secondary structure from patterns of chemical shifts. A. Toy-Palmer, S. Prytulla and H.J. Dyson
(1995) FEBS Lett. 365, 35-41.
60. Proton sharing
between cysteine thiols in Escherichia
coli thioredoxin: implications for the mechanism of reduction of protein
disulfides. M.-F. Jeng, A. Holmgren,
& H.J. Dyson (1995) Biochemistry 34,
10101-10105.
61. 1H, 13C and 15N
chemical shift references in biomolecular NMR.
D.S. Wishart, C.G. Bigam, J. Yao, F. Abildgaard, H.J. Dyson, E.
Oldfield, J.L. Markley, & B.D. Sykes (1995) J. Biomol. NMR 6,
135-140.
62. Direct measurement of the Asp-26 pKa for reduced Escherichia coli thioredoxin by 13C NMR. M.-F. Jeng and H. J. Dyson (1996) Biochemistry
35, 1-6.
63. Folding of
proteins and protein fragments. H.J.
Dyson & P.E. Wright (1996) In:
Encyclopedia of Nuclear Magnetic Resonance
(ed. D.M. Grant and R.K. Harris) John Wiley,
64. Thioredoxin and
glutaredoxin. H.J. Dyson (1996) In: Encyclopedia of Nuclear Magnetic
Resonance (ed. D.M. Grant and R.K.
Harris) John Wiley,
65. NMR structural
studies of flexible molecules. P.E.
Wright & 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.
66. Replacement of Trp-28 in Escherichia coli thioredoxin by site-directed mutagenesis affects
thermodynamic stability but not function.
I. Slaby, V. Cerna, M.-F. Jeng, H.J. Dyson and A. Holmgren (1996) J.
Biol. Chem. 271, 3091-3096.
67. Solution
conformation of an immunogenic peptide derived from the principal neutralizing
determinant of the HIV-2 envelope glycoprotein gp125. A.P. Campbell, B.D. Sykes, E. Norrby, N.
Assa-Munt and H. J. Dyson (1996) Folding
and Design 1, 157-165.
68. Insights into
protein folding from NMR. H.J. Dyson and
P.E. Wright (1996) Ann Rev. Phys. Chem.
47, 369-395.
69. NMR solution structure of Cu(I) rusticyanin
from Thiobacillus ferrooxidans:
Structural basis for the the extreme acid stability and redox potential. M. V. Botuyan, A. Toy-Palmer, J. Chung, R. C.
Blake II, P. Beroza, D.A. Case & H. J. Dyson (1996) J. Mol. Biol. 263,
752-767.
70. Structure-based design of a
constrained-peptide mimic of the HIV-1 V3 loop neutralization site. J.B. Ghiara, D. Ferguson, A.C. Satterthwait,
H.J. Dyson & I.A. Wilson (1996) J.
Mol. Biol. 266, 31-39.
71. 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, 303-306.
72. 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.
73. Effects of buried charged groups on cysteine
thiol ionization and reactivity in Escherichia
coli thioredoxin: Structural and
functional characterization of mutants of Asp 26 and
74. Absence of a stable
intermediate on the folding pathway of Protein A (B domain). Y. Bai, A. Karimi, H.J. Dyson and P.E. Wright
(1997) Protein Sci.6, 1449-1457.
75. Contribution of increased length and intact
capping sequences to the conformational preference for helix in a 31-residue
peptide from the C-terminal sequence of myohemerythrin. M.T. Reymond, S. Huo, B. Duggan, P.E. Wright
and H.J. Dyson (1997) Biochemistry36, 5234-5244.
76. 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.
77. PCR-based gene synthesis for protein
over-production. D. Casimiro, P.E.
Wright and H.J. Dyson (1997) Structure
5, 1407-1412.
78. Electron spin
envelope modulation spectra of Thiobacillus
ferrooxidans rusticyanin and a mutant lacking one of the copper ligands.
C.J. Bender, D. Casimiro and H.J. Dyson (1997) J. Chem. Soc. (Faraday) 93, 3967-3980.
79. Structure of the recombinant full-length
Syrian hamster prion protein PrP(29-231): the N-terminus is highly
flexible. D.G. Donne, J.H. Viles, J.
Chung, D. Groth, I. Mehlhorn, F.E. Cohen, S.B. Prusiner, P.E. Wright & H.J.
Dyson (1997) Proc. Natl. Acad. Sci. USA
94, 13452-13457.
80. 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.
81. Solution structure of the KIX domain of CBP
bound to the transactivation domain of CREB: a model for activator:coactivator
interactions I. Radhakrishnan, G.
Perez-Alvarado, D. Parker, H.J. Dyson, M. Montminy and P.E. Wright (1997) Cell 91, 741-752.
82. 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) Nature Struct. Biol. 5,
148-155.
83. A NOESY-HSQC
simulation program SPIRIT. L. Zhu, H.J.
Dyson and P.E. Wright (1998) J. Biomol.
NMR 11, 17-29.
84. Calculations of electrostatic interactions and
pKas in the active site of Escherichia
coli thioredoxin. V. Dillet, H.J.
Dyson and D. Bashford (1998) Biochemistry
37, 10298-10306.
85. Equilibrium NMR studies of unfolded and partly
folded proteins. H.J. Dyson and P.E.
Wright (1998) Nature Struct. Biol. 5, 499-503.
86. 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.
87. 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, & P.E. Wright (1998) Eur. J. Biochem. 255, 462-471.
88. 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.
89. 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.
90. The
identification of metal-binding ligand residues in metallo-b-lactamase from Bacteroides fragilis using NMR spectroscopy. S.D.B. Scrofani, P.E. Wright and H.J. Dyson
(1998) Protein Sci. 7, 2476-2479.
91. Glycosylation of threonine of the repeating
unit of RNA polymerase II confers a structural change. E. E. Simanek, D.-H. Huang, L. Pasternack, O.
Seitz, D.S. Millar, H.J. Dyson and C.-H. Wong (1998) J. Am. Chem. Soc. 120,
11567-11575.
92. NMR characterization of a single-cysteine
mutant of Escherichia coli
thioredoxin and a covalent thioredoxin-peptide complex. M.-F. Jeng, M.T.
Reymond, L.L. Tennant, A. Holmgren and H.J. Dyson (1998). Eur. J.
Biochem. 257, 299-308.
93. 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.
94. Quench-flow experiments combined with mass
spectrometry show that apomyoglobin folds through an obligatory intermediate.
V. Tsui, C. Garcia-Gonzalez, S. Cavagnero, G. Siuzdak, H.J. Dyson and P.E.
Wright (1999) Protein Sci. 8, 45-49.
95. Effect of H helix destabilizing mutations on
the kinetic and equilibrium folding of apomyoglobin. S. Cavagnero, H.J. Dyson and P.E. Wright.
(1999) J. Mol. Biol. 285, 269-282.
96. Copper binding to the prion protein. Structural implications of four identical
cooperative binding sites. J.H. Viles,
S.B. Prusiner, F.E. Cohen, D.D. Goodin, P.E. Wright and H.J. Dyson (1999) Proc. Natl Acad. Sci. USA 96, 2042-2047.
97. 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.
98. Structural analysis 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.R. Montminy and P.E. Wright (1999) J. Mol. Biol. 287,
859-865.
99. Association between the first two immunoglobulin-like
domains of the neural cell adhesion molecule N-CAM. A. 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.
100. Intrinsically unstructured proteins:
re-assessing the protein structure-function paradigm. P.E. Wright and H.J. Dyson (1999) J. Mol. Biol. 293, 321-331.
101. 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 & H.J. Dyson. (1999) J.
Pept. Res. 54, 344-352.
102. Inherent flexibility in a potent inhibitor of
blood coagulation, recombinant nematode anticoagulant protein c2. B.M. Duggan, H.J. Dyson & P.E. Wright
(1999) Eur. J. Biochem. 265, 539-548.
103. 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.
104. NMR
characterization of the metallo-b-lactamase
from Bacteroides fragilis and its
interaction with a tight-binding inhibitor: Role of a flexible 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.
105. Backbone resonance assignments for the Fv fragment of
the catalytic antibody NPN43C9 with bound p-nitrophenol. G. Kroon, M. Martinez-Yamout, J.F. Krebs,
John Chung, H.J. Dyson & P.E. Wright (1999) J. Biomol. NMR 15,
83-84.
106. Amide proton hydrogen exchange rates of sperm
whale myoglobin obtained from 15N-1H NMR spectra. S. Cavagnero, Y. Thériault, S.S. Narula, H.J.
Dyson & P.E. Wright. (2000) Protein
Sci. 9,186-193.
107. 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.
108. DNA-induced α-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.
109. Spectroscopic
methods. H.J. Dyson (2000) Encyclopedia of Life Sciences Macmillan
Online publication http://www.els.net./
110. Backbone HN, N, Ca, C’ and Cb assignments of the 19 kDa DHFR/NADPH complex at 9°C and
pH 7.6. E. Zaborowski, J. Chung, G.
Kroon, H.J. Dyson and P.E. Wright (2000) J.
Biomol. NMR 16, 349-350.
111. 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.
112. 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.
113. Identification of the regions involved in DNA binding
by the mouse PEBP2a protein. G.C. Perez-Alvarado, A. Munnerlyn, H.J.
Dyson, R. Grosschedl and
P.E. Wright (2000) FEBS Lett. 470, 125-130.
114.
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, P.E. Wright
(2000) Biochemistry 39, 5341-5348.
115. Conservation
of folding pathways in evolutionarily distant globin sequences. C. Nishimura, S. Prytulla, H.J. Dyson &
P.E. Wright (2000) Nature Struct. Biol.
7, 679-686.
116. 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.
117. 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.
118. 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.
119. 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 and H.J. Dyson (2000) J. Biomol.
NMR 18, 43-48.
120. Dynamics
of the metallo-b-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.
121. Molecular
basis for modulation of biological function by alternate splicing of the Wilms’
tumor suppressor protein. J.H. Laity,
H.J. Dyson and PE. Wright (2000) Proc.
Natl. Acad. Sci. USA 97,
11932-11935.
122. 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, 335-370.
123. 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.
124. NMR methods for the elucidation of the structure and
dynamics in disordered states. H.J. Dyson
and P.E. Wright (2001) Methods Enzymol.
339, 258-270.
125. Local
structural plasticity of the prion protein. Analysis of NMR relaxation
dynamics. J.H. Viles, D. Donne, G.J.A. Kroon, S.B. Prusiner, F.E. Cohen, H.J.
Dyson and P.E. Wright (2001) Biochemistry
40, 2743-2753.
126. 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.
127. NMR
structural and dynamic characterization of the acid-unfolded state of
apomyoglobin: a model system for the initial steps of folding. J. Yao, J. Chung, D. Eliezer, P.E. Wright and
H.J. Dyson (2001) Biochemistry 40, 3561-3571.
128. 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.
129. Genomic-scale comparison of sequence- and
structure-based methods of function prediction: Does structure provide
additional insight? J.S. Fetrow, N.
Siew, J.A. Di Gennaro, M. Martinez-Yamout, H.J. Dyson and J. Skolnick (2001) Protein Sci. 10, 1005-1014.
130. Sequence-dependent correction of random coil chemical
shifts. S. Schwarzinger, G.J.A. Kroon,
T.R. Foss, J. Chung, P.E. Wright and H.J. Dyson (2001). J. Am. Chem. Soc. 123,
2970-2978.
131. 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.
132. Structural
characterization of unfolded apo-plastocyanin by multi-dimensional NMR. Y. Bai, J. Chung, H.J. Dyson and P.E. Wright
(2001) Protein Sci. 10,
1056-1066.
133. 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.
134. 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.
135. 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. Atkins, J. Chung, S. Deechongkit, E. B. Little, G. M. Edelman, P.
E. Wright, B. A. Cunningham and H. J. Dyson (2001) J. Mol. Biol. 311, 161-172.
136. Structure and dynamics of disordered proteins. H.J. Dyson and P.E. Wright (2001) Encyclopedia
of NMR (in press).
137.
Conformational and dynamic characterization of the molten-globule state of an
apomyoglobin mutant with an altered folding pathway. S. Cavagnero, S.
Schwarzinger, H.J. Dyson and P.E. Wright (2001). Biochemistry
40, 14459-14467.
138. 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.
139. 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.
140. Coupling of folding and binding for unstructured proteins. H.J. Dyson and P.E. Wright (2002) Curr. Opin. Struct. Biol. 12, 54-60.
141. 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.
142. Synergistic folding of the interaction domain of the hypoxia-inducible factor-1a upon binding to the CH1 domain of CREB binding protein. S. Dames, M. Martinez-Yamout, R. N. DeGuzman, M. Allen, H.J. Dyson and P.E. Wright (2002) Proc. Natl. Acad. Sci. USA 99, 5271-5276.
143. Insights into the structure and dynamics of unfolded proteins from NMR. H. J. Dyson and P. E. Wright. (2002) Adv. Prot. Chem. 62, 311-340.
144. 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.
145. 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.
146. Molecular hinges during protein folding: residual structure and backbone dynamics of denatured states of apomyoglobin in acidic urea. S. Schwarzinger, P.E. Wright and H.J. Dyson. (2002) Biochemistry 41, 12681-12686.
147. Roles of phosphorylation and helix propensity in the binding of the KIX domain of CBP by constitutive (c-Myb) and inducible (CREB) activators. T. Zor, B.M. Mayr, H.J. Dyson and P.E. Wright (2002). J. Biol. Chem. 277, 42241-42248.
148. Cooperativity in transcription factor binding to the coactivator CBP: MLL binds to an allosteric site on the KIX domain. N.K. Goto, T. Zor, M. Martinez-Yamout, H.J. Dyson and P.E. Wright (2002). J. Biol. Chem. 277, 43168-43174.
149. Folding of a b-sheet protein monitored by real-time NMR spectroscopy. M. Mizuguchi, G. Kroon, H.J. Dyson and P.E. Wright (2003) J. Mol. Biol. 328, 1161-1171.
150. Plasmodium vivax peptides display conformational preferences for folded forms in solution. T.E. Lehmann, G. Kroon, M.A. Lorenzo, H. Bermúdez, H. Perez and H.J. Dyson (2003) J. Peptide Research 61, 252-262.
151. The role of a solvent-exposed
tryptophan in the recognition and binding of antibiotic substrates for a
metallo-b-lactamase. J.J.A. Huntley, W. Fast, S.J. Benkovic, P.E.
Wright and H.J. Dyson (2003). Protein Sci. 12, 1368-1375.
152. Solution structure of human estrogen related receptor-2 bound to an extended DNA half-site: monomeric binding depends on intramolecular protein-protein packing. M.D. Gearhart, S.M.A. Holmbeck, R.M. Evans, H.J. Dyson and P.E. Wright (2003) J. Mol. Biol. 327, 819-832.
153. 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 Sci. 12, 1386-1394.
154. Structure of the nuclear factor ALY: insights into post-transcriptional regulatory and mRNA export processes. G.C. Perez-Alvarado, M. Martinez-Yamout, M. Allen, R. Grosschedl, H.J. Dyson and P.E. Wright (2003) Biochemistry 42, 7348-7357.
155. 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.
156. 156. 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.
157. 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 Sci. 13, 203-210.
158. Effect of co-factor binding and loop conformation on fast methyl dynamics in DHFR. J.R. Schnell H.J. Dyson and P.E. Wright (2004). Biochemistry 43, 374-383.
159. Unfolded proteins and protein folding studied by NMR. H.J. Dyson and P.E. Wright (2004). Chemical Reviews 104, 3607-3622.
160. Structure, dynamics and catalytic function in dihydrofolate reductase. J.R. Schnell, H.J. Dyson and P.E. Wright (2004). Ann. Rev. Biophys. Biomol. Struct. 33, 119-140.
161. Interaction of the TAZ1 domain of 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.
162. 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 and N. Kuldell) Landes Biosciences. Chapter 17, pp 1-7.
163. Structural basis for recognition of the mRNA Type II AU-rich element by the tandem zinc finger domain of TIS11d. B.P. Hudson, M.A. Martinez-Yamout, J. Chung, H.J. Dyson, P.E. Wright (2004). Nature Struct. Biol. 11,257-264.
164. 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.
165. Activation of the redox-regulated chaperone Hsp33 by domain unfolding. P.C.F. Graf, M.A. Martinez-Yamout, S. VanHaerents, H. Lilie, H.J. Dyson and U. Jakob (2004). J. Biol. Chem. 279, 20529-20538.
166. Disulfide bonding arrangements in active forms of the somatomedin B domain of human vitronectin. Y. Kamikubo, R. DeGuzman, G. Kroon, S. Curriden, J. Neels, M.J. Churchill, P. Dawson, S. Oldziej, A. Jagielska, H.A. Scheraga, D.J. Loskutoff and H.J. Dyson (2004). Biochemistry 43, 6519-6534.
167. 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
168. The LEF-1 HMG 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.
169. Structural characterization of unfolded and partly folded states of apomyoglobin using residual dipolar couplings. R.M. Borges, H.J. Dyson and P.E. Wright (2004) J. Mol. Biol. 330, 1131-1142.
170. The zinc-dependent redox switch domain of the chaperone Hsp33 has a novel fold. H.-S. Won, L. Y. Low, R. N. De Guzman, M.A. Martinez-Yamout, U. Jakob and H.J. Dyson (2004). J. Mol. Biol. 341, 893-899.
171. ZZ Domain of CBP - a novel fold for a protein interaction module. G.B. Legge, M.A. Martinez-Yamout, G.J.A. Kroon, D. Hambly, H. J. Dyson and P.E. Wright (2004). J. Mol. Biol. 343, 1081-1093.
172. Conformational
changes in the active site loops of dihydrofolate reductase during the
catalytic cycle. R.P. Venkitakrishnan,
173. The isolated
CBP/p300 TAZ1 domain folds into a three dimensional structure in the absence of
its binding partners. R.N. De Guzman,
J.M. Wojciak, M.A.
174. Generation of
native-like models from limited NMR data, modern force fields and advanced
conformational sampling. J. Chen, H.-S. Won, W. Im, H.J. Dyson and
175. Intrinsically unstructured proteins and their functions. H.J. Dyson and P.E. Wright (2005). Nature Rev. Mol. Cell Biol. 6, 197-208.
176. Elucidation of the protein folding landscape by NMR. H.J. Dyson and P.E. Wright (2005). Methods Enzymol. 394, 299-321.
177. Backbone HN, N, Ca, C′ and Cb assignments of Escherichia coli SdiA1-171, the autoinducer binding domain of a quorum sensing protein. Y.Yao, M.A.Martinez-Yamout and H.J. Dyson (2005). J. Biomol. NMR 31, 373-374.
178. Enhanced picture of protein folding intermediates using organic solvents in HD exchange and quench flow experiments. C. Nishimura, H.J. Dyson and P.E. Wright (2005). Proc. Natl Acad. Sci. USA 102, 4765-4770.
179. Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis. D. McElheny, J.R. Schnell, J. Lansing, H.J. Dyson and P.E. Wright (2005). Proc. Natl. Acad. Sci. USA 102, 5032-5037.
180. 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.
181. Solution structure of the first two zinc finger domains of the double-stranded RNA-binding protein dsRBP-zfa. H. M. Möller, Maria A. Martinez-Yamout, H. J. Dyson and P. E. Wright (2005). J. Mol. Biol. 351, 718-730.
182. Structural basis for cooperative transcription factor binding to the CBP coactivator. R.N. De Guzman, N. Goto, H.J. Dyson and P.E. Wright (2006). J. Mol. Biol. 355, 1005-1013.
183. NMR solution structure of the peptide fragment 1-30, derived from mouse Doppel protein, in DHPC micelles. E. Papadopoulos, K. Oglęcka, L. Mäler, J. Jarvet, P.E. Wright, H.J. Dyson, A. Gräslund (2006). Biochemistry 45, 159-166.
184. 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.
185. 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.
186. Induced fit and “lock-and-key” recognition of 5S RNA by zinc fingers of transcription factor IIIA. B.M. Lee, J. Xu, M.D. Gearhart, B.K. Clarkson, M.A. MartinezYamout, H.J. Dyson, D.A. Case, J.M. Gottesfeld, and P.E. Wright (2006). J. Mol. Biol. 357, 275-291.
187. The reduced and denatured form of the somatomedin B domain of vitronectin refolds into a stable, biologically active form. Y. Kamikubo, G. Kroon, S.A. Curriden, H.J. Dyson and D.J. Loskutoff. Biochemistry 45, 3297-3306.
188. According to current textbooks, a well-defined three-dimensional structure is a prerequisite for the function of the protein. Is this correct? H.J. Dyson and P.E. Wright (2006) IUBMB Life 58, 107-109.
189. Localization of sites of interaction between p23 with 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.
190. An NMR perspective on enzyme dynamics. D.D. Boehr, H.J. Dyson and P.E. Wright (2006). Chem. Rev. 106, 3055-3079.
191. The dynamic energy landscape of dihydrofolate reductase catalysis. D.D. Boehr, D. McElheny, H. J. Dyson, P.E. Wright (2006). Science 313, 1638-1642.
192. Role of specific hydrophobic regions in initiating protein folding. H.J. Dyson, P.E. Wright, H.A. Scheraga (2006) Proc. Natl. Acad. Sci. USA 103, 13057-13061.
193. Solution structure of the Hdm2 C2H2C4 RING finger, a domain critical for ubiquitination of p53. M. Kostic, T. Matt, H.J. Dyson and P.E. Wright (2006) J. Mol. Biol. 363, 433-450.
194. Mechanism of coupled folding and binding of an intrinsically unstructured protein. K. Sugase, H.J. Dyson and P.E. Wright (2007) Nature 447, 1021-1025.
195. Embryonic neural
inducing factor Churchill is not a DNA-binding zinc finger: solution structure
reveals a solvent-exposed b-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
196. Structure of the zinc finger domain of the Wilms’ Tumor suppressor protein bound to DNA. R. Stoll, B.M. Lee, E. Debler, J.H. Laity, I.A. Wilson, H.J. Dyson and P.E. Wright (2007) J. Mol. Biol. 372, 1227-1245.
197. Structure
discrimination for the C-terminal domain of E. coli trigger
factor in solution. Y.
198. NMR detection of adventitious binding of xylose to the quorum-sensing protein SdiA of Escherichia coli. Y. Yao, T.J. Dickerson, M.S. Hixon and H. J. Dyson (2007). Bioorg. Med Chem. Lett. 17, 6202-6205.
199. Tailoring relaxation dispersion experiments for fast-associating protein complexes. K. Sugase, J.C. Lansing, H.J. Dyson and P.E. Wright (2007). J. Am. Chem. Soc. 129, 13406-13407.
200. NMR relaxation study of the complex formed between the nuclear coactivator binding domain of CBP and a fragment of the nuclear hormone receptor coactivator ACTR. M.-O. Ebert, S.-H. Bae, H.J. Dyson, P.E. Wright (2008) Biochemistry 47, 1299-1308.
201. Structural characterization of folding intermediates of the H64F mutant of apomyoglobin: stepwise stabilization of a native-like hydrophobic cluster. S. Schwarzinger, R. Mohana-Borges, G.J.A. Kroon, H.J. Dyson and P.E. Wright (2008) Protein Sci. 17, 313-321.
202. Modeling transient collapsed states of an unfolded protein to provide insights into early folding processes. D.J. Felitsky, M.A. Lietzow, H.J. Dyson and P.E. Wright (2008) Proc. Natl. Acad. Sci. USA (in press).
203. The
kinetic and equilibrium molten globule intermediates of apoleghemoglobin differ
in structure. C. Nishimura, P.E.
Wright and H.J. Dyson (2008) J. Mol.
Biol. (in press).
204. Hydrogen-deuterium exchange strategy for delineation of contact sites in protein complexes. H.J. Dyson, M. Kostic, J.J.Y. Liu and M.A. Martinez-Yamout (2008) FEBS Lett. (in press).