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PMID: 2696173 Published · ppublish English Journal Article Review

Barnase and barstar: two small proteins to fold and fit together.

Trends in biochemical sciences ·Vol. 14 ·No. 11 ·1989-11-00 ·Pages 450-4

Hartley RW

Abstract

Barnase and barstar are the extracellular ribonuclease and its intracellular inhibitor produced by Bacillus amyloliquefaciens. Both are small single-chain proteins and thus are suitable for application to the study of how a protein's sequence directs its fold. Barnase has neither disulfide bonds nor non-peptide components and unfolds reversibly in what closely approximates a two-state reaction. The genes for both these proteins have been cloned in E. coli. Expression of barstar is necessary to counter the lethal effect of expressed active barnase. Site-directed mutagenesis is being used to answer specific and general questions relating to protein folding and protein-protein interaction.

MeSH Terms
Amino Acid Sequence Bacillus/enzymology Bacterial Proteins/genetics,metabolism Cloning, Molecular Genes, Bacterial Molecular Sequence Data Protein Conformation Ribonucleases/antagonists & inhibitors,genetics,metabolism
Chemicals
Bacterial Proteins barstar protein, Bacillus amyloliquefaciens Ribonucleases Bacillus amyloliquefaciens ribonuclease
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Hartley R W
Article Info
Journal
Trends in biochemical sciences
Abbr.
Trends Biochem Sci
ISSN
0968-0004
Published
1989-11-00
Pages
450-4
Language
English
Region
England
NLM ID
7610674
Subset
IM
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