(Q57019346)

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Quantitative analysis of structure–activity relationships in engineered proteins by linear free-energy relationships

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Quantitative analysis of structure–activity relationships in engineered proteins by linear free-energy relationships (English)

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1

Alan R. Fersht

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Robin J. Leatherbarrow

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Tim N. C. Wells

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language of work or name

English

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publication date

July 1986

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Nature

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322

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6076

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284-286

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cites work

A primer for the Bema Hapothle. An empirical approach to the characterization of changing transition-state structures

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

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Hydrogen bonding and biological specificity analysed by protein engineering

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Transition-state stabilization in the mechanism of tyrosyl-tRNA synthetase revealed by protein engineering

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Hydrogen bonding in enzymatic catalysis analysed by protein engineering

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Use of binding energy in catalysis analyzed by mutagenesis of the tyrosyl-tRNA synthetase.

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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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10.1038/322284A0

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1018941941

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(Q57019346)

Quantitative analysis of structure–activity relationships in engineered proteins by linear free-energy relationships

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