Literature DB >> 7763976

Protein engineering for unusual environments.

F H Arnold1.   

Abstract

The ability to use proteins in unusual or non-natural environments greatly expands their potential applications in biotechnology. Because natural selection has neither maximized the stability of proteins nor optimized them to function under unusual conditions, there is considerable room for their improvement by protein engineering. Significant advances reported within the past year include a dramatic demonstration of a protein's ability to tolerate changes in its amino acid sequence, large increases in protein stability, and the use of random mutagenesis to obtain novel enzymatic properties. Approaches using random or site-directed mutagenesis have been successful in generating proteins able to function in an extended range of environments.

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Year:  1993        PMID: 7763976     DOI: 10.1016/0958-1669(93)90011-k

Source DB:  PubMed          Journal:  Curr Opin Biotechnol        ISSN: 0958-1669            Impact factor:   9.740


  4 in total

Review 1.  In vivo versus in vitro screening or selection for catalytic activity in enzymes and abzymes.

Authors:  J Fastrez
Journal:  Mol Biotechnol       Date:  1997-02       Impact factor: 2.695

2.  Interfacial activation-based molecular bioimprinting of lipolytic enzymes.

Authors:  I Mingarro; C Abad; L Braco
Journal:  Proc Natl Acad Sci U S A       Date:  1995-04-11       Impact factor: 11.205

3.  Is strong hydrogen bonding in the transition state enough to account for the observed rate acceleration in a mutant of papain?

Authors:  Y J Zheng; T C Bruice
Journal:  Proc Natl Acad Sci U S A       Date:  1997-04-29       Impact factor: 11.205

Review 4.  Protein Function Analysis through Machine Learning.

Authors:  Chris Avery; John Patterson; Tyler Grear; Theodore Frater; Donald J Jacobs
Journal:  Biomolecules       Date:  2022-09-06
  4 in total

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