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. (316)
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.
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.
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. (122)
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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) Biochemistry 36, 5234-5244.
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.
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.
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.
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.
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.