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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
1980-5-14
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pubmed:abstractText |
The pH dependence and the temperature dependence of the nuclear magnetic resonance spectrum of horse ferrocytochrome c are described. This protein is very stable; it maintains an ordered structure over the pH range 4 to 12 at 25 degrees C and over the temperature range 4 degrees C to 97 degrees C at pH 7.0. The dynamic characteristics of the conformation of ferrocytochrome c were investigated. Particular emphasis was laid on the aromatic resonances and resonances of methyl groups shifted far upfield. Tyr-48 and Phe-46 were found to be relatively immobile whilst a region of the protein close to Ile-57 was found to be relatively flexible.
|
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Feb
|
pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
103
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
|
pubmed:pagination |
513-21
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:6244160-Amino Acids,
pubmed-meshheading:6244160-Animals,
pubmed-meshheading:6244160-Cytochrome c Group,
pubmed-meshheading:6244160-Drug Stability,
pubmed-meshheading:6244160-Horses,
pubmed-meshheading:6244160-Hydrogen-Ion Concentration,
pubmed-meshheading:6244160-Magnetic Resonance Spectroscopy,
pubmed-meshheading:6244160-Protein Conformation,
pubmed-meshheading:6244160-Temperature
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pubmed:year |
1980
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pubmed:articleTitle |
Nuclear-magnetic-resonance studies of ferrocytochrome c. pH and temperature dependence.
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pubmed:publicationType |
Journal Article
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