Dyson HJ - Search Results

1

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.

Oldstone MB, Tishon A, Lewicki H, Dyson HJ, Feher VA, Assa-Munt N, Wright PE. Oldstone MB, et al. Among authors: dyson hj. J Virol. 1991 Apr;65(4):1727-34. doi: 10.1128/JVI.65.4.1727-1734.1991. J Virol. 1991. PMID: 2002540 Free PMC article.

2

Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin.

Dyson HJ, Merutka G, Waltho JP, Lerner RA, Wright PE. Dyson HJ, et al. J Mol Biol. 1992 Aug 5;226(3):795-817. doi: 10.1016/0022-2836(92)90633-u. J Mol Biol. 1992. PMID: 1507227

3

Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. II. Plastocyanin.

Dyson HJ, Sayre JR, Merutka G, Shin HC, Lerner RA, Wright PE. Dyson HJ, et al. J Mol Biol. 1992 Aug 5;226(3):819-35. doi: 10.1016/0022-2836(92)90634-v. J Mol Biol. 1992. PMID: 1507228

4

Antigen-antibody interactions: an NMR approach.

Wright PE, Dyson HJ, Lerner RA, Riechmann L, Tsang P. Wright PE, et al. Among authors: dyson hj. Biochem Pharmacol. 1990 Jul 1;40(1):83-8. doi: 10.1016/0006-2952(90)90182-k. Biochem Pharmacol. 1990. PMID: 1695509

5

Immunogenic peptides corresponding to the dominant antigenic region alanine-597 to cysteine-619 in the transmembrane protein of simian immunodeficiency virus have a propensity to fold in aqueous solution.

Dyson HJ, Norrby E, Hoey K, Parks DE, Lerner RA, Wright PE. Dyson HJ, et al. Biochemistry. 1992 Feb 11;31(5):1458-63. doi: 10.1021/bi00120a024. Biochemistry. 1992. PMID: 1737004

6

Defining solution conformations of small linear peptides.

Dyson HJ, Wright PE. Dyson HJ, et al. Annu Rev Biophys Biophys Chem. 1991;20:519-38. doi: 10.1146/annurev.bb.20.060191.002511. Annu Rev Biophys Biophys Chem. 1991. PMID: 1867725 Review. No abstract available.

7

Solution conformational preferences of immunogenic peptides derived from the principal neutralizing determinant of the HIV-1 envelope glycoprotein gp120.

Chandrasekhar K, Profy AT, Dyson HJ. Chandrasekhar K, et al. Among authors: dyson hj. Biochemistry. 1991 Sep 24;30(38):9187-94. doi: 10.1021/bi00102a009. Biochemistry. 1991. PMID: 1892828

8

Polypeptide backbone resonance assignments and secondary structure of Bacillus subtilis enzyme IIIglc determined by two-dimensional and three-dimensional heteronuclear NMR spectroscopy.

Fairbrother WJ, Cavanagh J, Dyson HJ, Palmer AG 3rd, Sutrina SL, Reizer J, Saier MH Jr, Wright PE. Fairbrother WJ, et al. Among authors: dyson hj. Biochemistry. 1991 Jul 16;30(28):6896-907. doi: 10.1021/bi00242a013. Biochemistry. 1991. PMID: 1906345

9

Assignment of the 15N NMR spectra of reduced and oxidized Escherichia coli thioredoxin.

Chandrasekhar K, Krause G, Holmgren A, Dyson HJ. Chandrasekhar K, et al. Among authors: dyson hj. FEBS Lett. 1991 Jun 24;284(2):178-83. doi: 10.1016/0014-5793(91)80679-w. FEBS Lett. 1991. PMID: 2060637 Free article.

10

The conformational restriction of synthetic vaccines for malaria.

Satterthwait AC, Chiang LC, Arrhenius T, Cabezas E, Zavala F, Dyson HJ, Wright PE, Lerner RA. Satterthwait AC, et al. Among authors: dyson hj. Bull World Health Organ. 1990;68 Suppl(Suppl):17-25. Bull World Health Organ. 1990. PMID: 2094582 Free PMC article. Review.

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