Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1995-9-8
pubmed:abstractText
The cytochrome c' are paramagnetic heme proteins generally consisting of two identical 14 kDa subunits. The recent assignment of the 1H and 15N resonances of the Rhodobacter capsulatus ferricytochrome c' has allowed characterization of the dynamic properties by measurement of the heteronuclear NOE for each resolved amide group. The relative importance of fast local motion and paramagnetic effect on nuclear relaxation were distinguished by comparison of the measured heteronuclear NOE with that of the overall experimental average. We show that the average experimental value of -0.16 corresponds to the rigid body motion expected for a spherical complex of 28 kDa. Residues 3-5, 50-55 and 69-70 exhibit decreased heteronuclear NOE due to local motions on a fast time scale with respect to molecular tumbling. Based on the X-ray crystal structure of the homologous cytochrome c' from Chromatium vinosum, the mobile regions correspond to the N-terminus of helix-1 and 2 regions of nonregular secondary structure located between helices-2 and -3.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
368
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
519-22
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Characterization of the dynamic properties of Rhodobacter capsulatus ferricytochrome c'--a 28 kDa paramagnetic heme protein.
pubmed:affiliation
Institut de Biologie Structurale Jean-Pierre Ebel (CNRS-CEA), Grenoble, France.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't