Onuffer JJ - Search Results

1

Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis.

Onuffer JJ, Kirsch JF. Onuffer JJ, et al. Protein Sci. 1995 Sep;4(9):1750-7. doi: 10.1002/pro.5560040910. Protein Sci. 1995. PMID: 8528073 Free PMC article.

2

Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase.

Malashkevich VN, Onuffer JJ, Kirsch JF, Jansonius JN. Malashkevich VN, et al. Among authors: onuffer jj. Nat Struct Biol. 1995 Jul;2(7):548-53. doi: 10.1038/nsb0795-548. Nat Struct Biol. 1995. PMID: 7664122

3

Characterization of the apparent negative co-operativity induced in Escherichia coli aspartate aminotransferase by the replacement of Asp222 with alanine. Evidence for an extremely slow conformational change.

Onuffer JJ, Kirsch JF. Onuffer JJ, et al. Protein Eng. 1994 Mar;7(3):413-24. doi: 10.1093/protein/7.3.413. Protein Eng. 1994. PMID: 8177890

4

The use of natural and unnatural amino acid substrates to define the substrate specificity differences of Escherichia coli aspartate and tyrosine aminotransferases.

Onuffer JJ, Ton BT, Klement I, Kirsch JF. Onuffer JJ, et al. Protein Sci. 1995 Sep;4(9):1743-9. doi: 10.1002/pro.5560040909. Protein Sci. 1995. PMID: 8528072 Free PMC article.

5

Characterization of tryptophan phosphorescence of aspartate aminotransferase from Escherichia coli.

Cioni P, Onuffer JJ, Strambini GB. Cioni P, et al. Among authors: onuffer jj. Eur J Biochem. 1992 Oct 15;209(2):759-64. doi: 10.1111/j.1432-1033.1992.tb17345.x. Eur J Biochem. 1992. PMID: 1425679 Free article.

6

Effect of single amino acid replacements on the folding and stability of dihydrofolate reductase from Escherichia coli.

Perry KM, Onuffer JJ, Touchette NA, Herndon CS, Gittelman MS, Matthews CR, Chen JT, Mayer RJ, Taira K, Benkovic SJ, et al. Perry KM, et al. Among authors: onuffer jj. Biochemistry. 1987 May 19;26(10):2674-82. doi: 10.1021/bi00384a004. Biochemistry. 1987. PMID: 3300767

7

Effects of the phenylalanine-22----leucine, glutamic acid-49----methionine, glycine-234----aspartic acid, and glycine-234----lysine mutations on the folding and stability of the alpha subunit of tryptophan synthase from Escherichia coli.

Beasty AM, Hurle MR, Manz JT, Stackhouse T, Onuffer JJ, Matthews CR. Beasty AM, et al. Among authors: onuffer jj. Biochemistry. 1986 May 20;25(10):2965-74. doi: 10.1021/bi00358a035. Biochemistry. 1986. PMID: 2872918

8

Folding of homologous proteins: conservation of the folding mechanism of the alpha subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrids.

Stackhouse TM, Onuffer JJ, Matthews CR, Ahmed SA, Miles EW. Stackhouse TM, et al. Among authors: onuffer jj. Biochemistry. 1988 Jan 26;27(2):824-32. doi: 10.1021/bi00402a050. Biochemistry. 1988. PMID: 3280027

9

Long-range electrostatic interactions can influence the folding, stability, and cooperativity of dihydrofolate reductase.

Perry KM, Onuffer JJ, Gittelman MS, Barmat L, Matthews CR. Perry KM, et al. Among authors: onuffer jj. Biochemistry. 1989 Sep 19;28(19):7961-8. doi: 10.1021/bi00445a061. Biochemistry. 1989. PMID: 2692706

10

The role of protein folding in the evolution of protein sequences.

Stackhouse T, Onuffer JJ, Matthews CR, Ahmed SA, Miles EW. Stackhouse T, et al. Among authors: onuffer jj. Cold Spring Harb Symp Quant Biol. 1987;52:537-44. doi: 10.1101/sqb.1987.052.01.061. Cold Spring Harb Symp Quant Biol. 1987. PMID: 3331344 No abstract available.

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