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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
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pubmed:dateCreated |
1998-9-18
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pubmed:abstractText |
It has been suggested that three partially unfolded forms detected in a native state hydrogen exchange study of oxidized cytochrome c may represent sequential intermediates in an unfolding-refolding pathway. To better define the structure of each intermediate a 'stability labeling' method was used in which the stability of a given segment against unfolding was changed. The condition--folded or unfolded--of the stability-labeled segment in each intermediate could then be determined. The structures found are discrete and native-like and are just those necessary for a sequential pathway.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1072-8368
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
774-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9731770-Animals,
pubmed-meshheading:9731770-Binding Sites,
pubmed-meshheading:9731770-Cytochrome c Group,
pubmed-meshheading:9731770-Heme,
pubmed-meshheading:9731770-Horses,
pubmed-meshheading:9731770-Hydrogen,
pubmed-meshheading:9731770-Magnetic Resonance Spectroscopy,
pubmed-meshheading:9731770-Methionine,
pubmed-meshheading:9731770-Models, Molecular,
pubmed-meshheading:9731770-Oxidation-Reduction,
pubmed-meshheading:9731770-Protein Conformation,
pubmed-meshheading:9731770-Protein Denaturation,
pubmed-meshheading:9731770-Protein Folding,
pubmed-meshheading:9731770-Thermodynamics
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pubmed:year |
1998
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pubmed:articleTitle |
Evidence for an unfolding and refolding pathway in cytochrome c.
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pubmed:affiliation |
Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia 19104, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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