|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
2
|
|
pubmed:dateCreated |
1999-7-30
|
|
pubmed:abstractText |
The thermal inactivation rates of a set of 20 cysteine-substituted variants of the integral membrane protein diacylglycerol kinase were measured. Two of the mutations, I53C and I70C, were found to significantly prolong the half-life of the enzyme in detergent solution. By combining the single mutants to create a double mutant, I53C/I70C, the half-life of the enzyme was improved from less than a minute at 70 degrees C to 51 minutes. These results demonstrate that individual side-chain substitutions can significantly improve the properties of membrane proteins in detergent solution.
|
|
pubmed:grant |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jul
|
|
pubmed:issn |
0022-2836
|
|
pubmed:author |
|
|
pubmed:copyrightInfo |
Copyright 1999 Academic Press.
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
9
|
|
pubmed:volume |
290
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
559-64
|
|
pubmed:dateRevised |
2008-11-21
|
|
pubmed:meshHeading |
pubmed-meshheading:10390353-Amino Acid Substitution,
pubmed-meshheading:10390353-Circular Dichroism,
pubmed-meshheading:10390353-Cysteine,
pubmed-meshheading:10390353-Diacylglycerol Kinase,
pubmed-meshheading:10390353-Diglycerides,
pubmed-meshheading:10390353-Disulfides,
pubmed-meshheading:10390353-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:10390353-Enzyme Stability,
pubmed-meshheading:10390353-Escherichia coli,
pubmed-meshheading:10390353-Half-Life,
pubmed-meshheading:10390353-Hot Temperature,
pubmed-meshheading:10390353-Kinetics,
pubmed-meshheading:10390353-Membrane Proteins,
pubmed-meshheading:10390353-Mutagenesis,
pubmed-meshheading:10390353-Protein Conformation,
pubmed-meshheading:10390353-Protein Denaturation,
pubmed-meshheading:10390353-Protein Engineering,
pubmed-meshheading:10390353-Thermodynamics
|
|
pubmed:year |
1999
|
|
pubmed:articleTitle |
Changing single side-chains can greatly enhance the resistance of a membrane protein to irreversible inactivation.
|
|
pubmed:affiliation |
Department of Chemistry and Biochemistry and Laboratory of Structural Biology and Molecular Medicine, UCLA, 405 Hilgard Avenue, Los Angeles, CA, 90095-1570, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
|
