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.