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.
Differential hydration of side chain protons in a short peptide in a highly populated Type VI turn conformation.J. Yao, R. Bruschweiler, 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. Oglecka, L. Maler, J. Jarvet, P.E. Wright, H.J. Dyson, A. Graslund (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. Barany-Wallje, P. Sonderby, L.H. Kristensen, M. Martinez-Yamout, H.J. Dyson, P.E. Wright, F.M. Poulsen, L. Maler, A. Graslund and B.B. Kragelund (2008) Biochemistry 47, 13428-13437.
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.