Hydrogen bonding and biological specificity analysed by protein engineering (Q34192392)

31 July 2017

title

Hydrogen bonding and biological specificity analysed by protein engineering (English)

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1

Fersht AR

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Shi JP

2

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Knill-Jones J

3

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Lowe DM

4

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Wilkinson AJ

5

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Blow DM

6

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Brick P

7

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Carter P

8

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Waye MM

9

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Winter G

10

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language of work or name

English

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publication date

1 March 1985

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volume

314

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issue

6008

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page(s)

235-238

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Some factors in the interpretation of protein denaturation

31 July 2017

cites work

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7 January 2021

Demonstration of two reaction pathways for the aminoacylation of tRNA. Application of the pulsed quenched flow technique

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7 January 2021

Site-directed mutagenesis as a probe of enzyme structure and catalysis: tyrosyl-tRNA synthetase cysteine-35 to glycine-35 mutation

1 reference

7 January 2021

Binding of tyrosine, adenosine triphosphate and analogues to crystalline tyrosyl transfer RNA synthetase

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7 January 2021

Amino acid activation in crystalline tyrosyl-tRNA synthetase from Bacillus stearothermophilus

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7 January 2021

Tyrosyl-tRNA synthetase forms a mononucleotide-binding fold

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7 January 2021

Redesigning enzyme structure by site-directed mutagenesis: tyrosyl tRNA synthetase and ATP binding

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7 January 2021

A large increase in enzyme–substrate affinity by protein engineering

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7 January 2021

The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus)

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7 January 2021

Interaction of crystalline tyrosyl-tRNA synthetase with adenosine, adenosine monophosphate, adenosine triphosphate and pyrophosphate in the presence of tyrosinol

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7 January 2021

Cysteinyl-tRNA synthetase from Escherichia coli does not need an editing mechanism to reject serine and alanine. High binding energy of small groups in specific molecular interactions

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7 January 2021

Evidence for the double-sieve editing mechanism in protein synthesis. Steric exclusion of isoleucine by valyl-tRNA synthetases

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7 January 2021

Deletion mutagenesis using an ‘M13 splint’: the N-terminal structural domain of tyrosyl-tRNA synthetase (B. stearothermophilus) catalyses the formation of tyrosyl adenylate

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7 January 2021

Probing the limits of protein-amino acid side chain recognition with the aminoacyl-tRNA synthetases. Discrimination against phenylalanine by tyrosyl-tRNA synthetases

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7 January 2021

Identifiers

DOI

10.1038/314235A0

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Dimensions Publication ID

31 July 2017

1053524488

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