Dyson HJ - Search Results

1

Comparison of the hydrogen-exchange behavior of reduced and oxidized Escherichia coli thioredoxin.

Jeng MF, Dyson HJ. Jeng MF, et al. Among authors: dyson hj. Biochemistry. 1995 Jan 17;34(2):611-9. doi: 10.1021/bi00002a028. Biochemistry. 1995. PMID: 7819256

2

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

3

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

4

Proton-transfer effects in the active-site region of Escherichia coli thioredoxin using two-dimensional 1H NMR.

Dyson HJ, Tennant LL, Holmgren A. Dyson HJ, et al. Biochemistry. 1991 Apr 30;30(17):4262-8. doi: 10.1021/bi00231a023. Biochemistry. 1991. PMID: 1850621

5

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

6

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

7

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.

8

Three-dimensional solution structure of the reduced form of Escherichia coli thioredoxin determined by nuclear magnetic resonance spectroscopy.

Dyson HJ, Gippert GP, Case DA, Holmgren A, Wright PE. Dyson HJ, et al. Biochemistry. 1990 May 1;29(17):4129-36. doi: 10.1021/bi00469a016. Biochemistry. 1990. PMID: 2193685

9

Conformational preferences of synthetic peptides derived from the immunodominant site of the circumsporozoite protein of Plasmodium falciparum by 1H NMR.

Dyson HJ, Satterthwait AC, Lerner RA, Wright PE. Dyson HJ, et al. Biochemistry. 1990 Aug 28;29(34):7828-37. doi: 10.1021/bi00486a008. Biochemistry. 1990. PMID: 2261440

10

Assignment of the proton NMR spectrum of reduced and oxidized thioredoxin: sequence-specific assignments, secondary structure, and global fold.

Dyson HJ, Holmgren A, Wright PE. Dyson HJ, et al. Biochemistry. 1989 Aug 22;28(17):7074-87. doi: 10.1021/bi00443a044. Biochemistry. 1989. PMID: 2684270

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