Structure of the Wilms Tumor Suppressor by Stoll, R., Lee, B.M., Debler, E.W., Laity, J.H., Wilson, I.A., Dyson, H.J., Wright, P.E.

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Three-dimensional solution structure of the reduced form of Escherichia coli thioredoxin determined by nuclear magnetic resonance spectroscopy by Dyson, H. Jane, Gippert, Garry P, Case, David A, Holmgren, Arne, Wright, Peter E

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Assignment of the proton NMR spectrum of reduced and oxidized thioredoxin: sequence-specific assignments, secondary structure, and global fold by Dyson, H. Jane, Holmgren, Arne, Wright, Peter E

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Active conformation of an insect neuropeptide family by Nachman, R.J. (Veterinary Toxicology and Entomology Research Laboratory, ARS, USDA, College Station, TX), Roberts, V.A, Dyson, H.J, Holman, G.M, Tainer, J.A

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Proton-transfer effects in the active-site region of Escherichia coli thioredoxin using two-dimensional sup 1 H NMR by Dyson, H.J., Tennant, L.L., Holmgren, A.

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Plasmodium vivax CS peptides display conformational preferences for folded forms in solution by Lehmann, T.E., Kroon, G., Dyson, H.J., Lorenzo, M.A., Bermúdez, H., Perez, H.

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Conformational preferences of synthetic peptides derived from the immunodominant site of the circumsporozoite protein of Plasmodium falciparum by sup 1 H NMR by Dyson, H.J., Satterthwait, A.C., Lerner, R.A., Wright, P.E.

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Polypeptide backbone resonance assignments and secondary structure of Bacillus subtilis enzyme III sup glc determined by two-dimensional and three-dimensional heteronuclear NMR spe... by Fairbrother, W.J., Cavanagh, J., Dyson, H.J., Palmer, A.G. III, Wright, P.E., Sutrina, S.L., Reizer, J., Saier, M.H. Jr

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Proton NMR studies of the solution conformations of an analog of the C-peptide of ribonuclease A by Osterhout, John J, Baldwin, Robert L, York, Eunice J, Stewart, John M, Dyson, H. Jane, Wright, Peter E

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