Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
1981-4-13
|
| pubmed:abstractText |
The resonances of Phe 82 and Phe 10 in the nuclear magnetic resonance spectra of horse cytochrome c are reassigned using nuclear Overhauser enhancements. The reassignments provide new information about the oxidation state linked conformation change of cytochrome c. The region of the protein now known to be affected by the change extends to the part of the protein close to Phe 10.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
0162-0134
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
13
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
347-52
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:6257839-Animals,
pubmed-meshheading:6257839-Cytochrome c Group,
pubmed-meshheading:6257839-Horses,
pubmed-meshheading:6257839-Magnetic Resonance Spectroscopy,
pubmed-meshheading:6257839-Oxidation-Reduction,
pubmed-meshheading:6257839-Phenylalanine,
pubmed-meshheading:6257839-Protein Conformation
|
| pubmed:year |
1980
|
| pubmed:articleTitle |
Nuclear magnetic resonance studies of the phenylalanine residues of eukaryotic cytochrome c.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|