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.
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.
Defining solution conformations of small linear peptides. H.J. Dyson & P.E. Wright (1991) Ann. Rev. Biophys. Biophys. Chem. 20, 519-538.
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.
Peptide conformation and protein folding. H.J. Dyson & P.E. Wright (1993) Curr. Opin. Struct. Biol. 3, 60-65.
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.,
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.
Antigenic peptides. H.J. Dyson & P.E. Wright (1995) FASEB J. 9, 37-42.
NMR of thioredoxin and glutaredoxin. H.J. Dyson (1995) Methods Enzymol. 252, 293-306.
Insights into protein folding from NMR. H.J. Dyson and P.E. Wright (1996) Ann Rev. Phys. Chem. 47, 369-395.
Equilibrium NMR studies of unfolded and partly folded proteins. H.J. Dyson and P.E. Wright (1998) Nature Struct. Biol. 5, 499-503.
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. P.E. Wright and H.J. Dyson (1999) J. Mol. Biol. 293, 321-331.
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.
Coupling of folding and binding for unstructured proteins. H.J. Dyson and P.E. Wright (2002) Curr. Opin. Struct. Biol. 12, 54-60.
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.
Unfolded proteins and protein folding studied by NMR. H.J. Dyson and P.E. Wright (2004). Chemical Reviews 104, 3607-3622.
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.
Elucidation of the protein folding landscape by NMR. H.J. Dyson and P.E. Wright (2005). Methods Enzymol. 394, 299-321.
Intrinsically unstructured proteins and their functions. H.J. Dyson and P.E. Wright (2005). Nature Reviews 6, 197-208.
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.
An NMR perspective on enzyme dynamics. D.D. Boehr, H.J. Dyson and P.E. Wright (2006). Chem. Rev. 106, 3055-3079.
Linking folding and binding. P.E. Wright and H.J. Dyson (2009) Curr. Opin. Struct. Biol. 19, 31-38.
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, F. Hirata, Y. Goto, M. Kataoka and M. Terazima,
eds)
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)