Protein engineering 20 years on

J A  Brannigan; A J  Wilkinson

doi:10.1038/nrm975

Protein engineering 20 years on

J A Brannigan, A J Wilkinson

Chemistry

Research output: Contribution to journal › Literature review › peer-review

Abstract

It is 20 years since site-directed mutagenesis was first used to modify the active site of an enzyme of known structure and mechanism. Since then, this method has contributed far-reaching insights into catalysis, specificity, stability and folding of proteins. Engineered proteins are now being used in industry and for the improved treatment of human disease.

Original language	English
Pages (from-to)	964-970
Number of pages	8
Journal	Nature reviews. Molecular cell biology
Volume	3
Issue number	12
DOIs	https://doi.org/10.1038/nrm975
Publication status	Published - Dec 2002

Keywords

SITE-DIRECTED MUTAGENESIS
TRANSFER-RNA-SYNTHETASE
LACTATE-DEHYDROGENASE FRAMEWORK
TRANSITION-STATE
IN-VITRO
SUBSTRATE-SPECIFICITY
MOLECULAR EVOLUTION
BLOOD SUBSTITUTES
ESCHERICHIA-COLI
ENZYME CATALYSIS

Access to Document

10.1038/nrm975

Cite this

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title = "Protein engineering 20 years on",

abstract = "It is 20 years since site-directed mutagenesis was first used to modify the active site of an enzyme of known structure and mechanism. Since then, this method has contributed far-reaching insights into catalysis, specificity, stability and folding of proteins. Engineered proteins are now being used in industry and for the improved treatment of human disease.",

keywords = "SITE-DIRECTED MUTAGENESIS, TRANSFER-RNA-SYNTHETASE, LACTATE-DEHYDROGENASE FRAMEWORK, TRANSITION-STATE, IN-VITRO, SUBSTRATE-SPECIFICITY, MOLECULAR EVOLUTION, BLOOD SUBSTITUTES, ESCHERICHIA-COLI, ENZYME CATALYSIS",

author = "Brannigan, {J A} and Wilkinson, {A J}",

year = "2002",

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doi = "10.1038/nrm975",

language = "English",

volume = "3",

pages = "964--970",

journal = "Nature reviews. Molecular cell biology",

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AU - Brannigan, J A

AU - Wilkinson, A J

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N2 - It is 20 years since site-directed mutagenesis was first used to modify the active site of an enzyme of known structure and mechanism. Since then, this method has contributed far-reaching insights into catalysis, specificity, stability and folding of proteins. Engineered proteins are now being used in industry and for the improved treatment of human disease.

AB - It is 20 years since site-directed mutagenesis was first used to modify the active site of an enzyme of known structure and mechanism. Since then, this method has contributed far-reaching insights into catalysis, specificity, stability and folding of proteins. Engineered proteins are now being used in industry and for the improved treatment of human disease.

KW - SITE-DIRECTED MUTAGENESIS

KW - TRANSFER-RNA-SYNTHETASE

KW - LACTATE-DEHYDROGENASE FRAMEWORK

KW - TRANSITION-STATE

KW - IN-VITRO

KW - SUBSTRATE-SPECIFICITY

KW - MOLECULAR EVOLUTION

KW - BLOOD SUBSTITUTES

KW - ESCHERICHIA-COLI

KW - ENZYME CATALYSIS

U2 - 10.1038/nrm975

DO - 10.1038/nrm975

M3 - Literature review

VL - 3

SP - 964

EP - 970

JO - Nature reviews. Molecular cell biology

JF - Nature reviews. Molecular cell biology

SN - 1471-0072

IS - 12

ER -