Protein Folding/Unfolded Proteins

Spin state and unfolding equilibria of ferricytochrome c in acidic solutions. H.J. Dyson & J.K. Beattie (1982) J. Biol. Chem. 257, 2267-2273.

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

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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

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

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.

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.

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.

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.

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.

Role of specific hydrophobic regions in initiating protein folding. H.A. Scheraga, P.E. Wright, H.J. Dyson (2006) Proc. Natl. Acad. Sci. USA 103, 13057-13061.

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.

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.

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 105, 6278-6283.

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. 378, 715-725.

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. Takahashi, H. J. Dyson and P. E. Wright (2008) Proc. Natl. Acad. Sci. USA 105, 13859-13864.

Amylin proprotein processing generates progressively more amyloidogenic peptides that initially sample the helical state. I.T. Yonemoto, G.J.A. Kroon, H.J. Dyson, W.E. Balch and J.W. Kelly (2008) Biochemistry 47, 9900-9910.

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

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, F. Hirata, Y. Goto, M. Kataoka and M. Terazima, eds) Ch. 6, pp 123-136.

Evaluating b-turn mimics as b-sheet folding nucleators. A.A. Fuller, D. Du, F. Liu, J.E. Davoren, G. Bhabha, G. Kroon, D.A. Case, H.J. Dyson, E.T. Powers, P. Wipf, M. Gruebele and J.W. Kelly (2009) Proc. Natl. Acad. Sci. USA 106, 11067-11072.)

Consequences of stabilizing the natively disordered F helix for the folding pathway of apomyoglobin. C. Nishimura, H.J. Dyson and P.E. Wright (2011) J. Mol. Biol. 411, 248-263.