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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1994-9-23
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pubmed:abstractText |
Staphylococcal nuclease is a well-developed model system for analyzing the effects of mutations on protein folding and stability. Substitution of glycine 88 with valine (Gly88Val) destabilizes staphylococcal nuclease by 1.0 kcal mole-1 and reduces its sensitivity to the denaturant guanidine hydrochloride, a phenomenon which may indicate an increase in residual structure in the denatured state. To assess its effects on denatured state structure, the Gly88Val mutation was incorporated into a 136 residue nonsense fragment which has been developed as a model of the wild type denatured state.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0969-2126
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
121-34
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8069625-Amino Acid Sequence,
pubmed-meshheading:8069625-Calorimetry,
pubmed-meshheading:8069625-Cloning, Molecular,
pubmed-meshheading:8069625-Enzyme Stability,
pubmed-meshheading:8069625-Escherichia coli,
pubmed-meshheading:8069625-Glycine,
pubmed-meshheading:8069625-Magnetic Resonance Spectroscopy,
pubmed-meshheading:8069625-Micrococcal Nuclease,
pubmed-meshheading:8069625-Models, Molecular,
pubmed-meshheading:8069625-Molecular Sequence Data,
pubmed-meshheading:8069625-Mutagenesis, Site-Directed,
pubmed-meshheading:8069625-Point Mutation,
pubmed-meshheading:8069625-Protein Conformation,
pubmed-meshheading:8069625-Protein Denaturation,
pubmed-meshheading:8069625-Protein Structure, Secondary,
pubmed-meshheading:8069625-Recombinant Proteins,
pubmed-meshheading:8069625-Valine
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pubmed:year |
1993
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pubmed:articleTitle |
NMR analysis of the residual structure in the denatured state of an unusual mutant of staphylococcal nuclease.
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pubmed:affiliation |
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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