Investigation of Half-of-Reactivity in Trna Synthetase - Eric First

Abstract

Funding Agency

Agency: National Institute of Health (NIH)
Institute: National Institute of General Medical Sciences (NIGMS)
Type: Postdoctoral Individual National Research Service Award (F32)
Project #: 5F32GM012023-03X1
Application #: 3042647
Study Section: (BI)

Project Start: 1989-09-15
Project End
Budget Start: 1989-09-15
Budget End: 1990-09-14
Support Year: 3
Fiscal Year: 1989
Total Cost
Indirect Cost

Institution

Name: University of Cambridge
Department
Type
DUNS #: 226552610

City: Cambridge
State
Country: United Kingdom
Zip Code: CB2 1TN

Related projects


NIH 1989 F32 GM	Investigation of Half-of-Reactivity in Trna Synthetase First, Eric A. / University of Cambridge
NIH 1989 F32 GM	Investigation of Half-of-Reactivity in Trna Synthetase First, Eric A. / University of Cambridge
NIH 1988 F32 GM	Investigation of Half-of-Reactivity in Trna Synthetase First, Eric A. / University of Cambridge
NIH 1988 F32 GM	Investigation of Half-of-Reactivity in Trna Synthetase First, Eric A. / University of Cambridge
NIH 1987 F32 GM	Investigation of Half-of-Reactivity in Trna Synthetase First, Eric A. / University of London
NIH 1987 F32 GM	Investigation of Half-of-Reactivity in Trna Synthetase First, Eric A. / University of London

Publications

First, E A; Fersht, A R (1995) Analysis of the role of the KMSKS loop in the catalytic mechanism of the tyrosyl-tRNA synthetase using multimutant cycles. Biochemistry 34:5030-43

First, E A; Fersht, A R (1993) Mutation of lysine 233 to alanine introduces positive cooperativity into tyrosyl-tRNA synthetase. Biochemistry 32:13651-7

First, E A; Fersht, A R (1993) Involvement of threonine 234 in catalysis of tyrosyl adenylate formation by tyrosyl-tRNA synthetase. Biochemistry 32:13644-50

First, E A; Fersht, A R (1993) Mutational and kinetic analysis of a mobile loop in tyrosyl-tRNA synthetase. Biochemistry 32:13658-63

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