Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
37
pubmed:dateCreated
1991-10-24
pubmed:abstractText
The interaction of cytochrome c with negatively charged lipids has been studied by resonance Raman spectroscopy of the protein heme group and 31P NMR of the phospholipid headgroups. The gel-to-fluid-phase transition of dimyristoylphosphatidylglycerol induces shifts in the conformational and coordination equilibria of the bound cytochrome c, as recorded by the resonance Raman spectra in the fingerprint and marker band regions. Conformational and coordination shifts of the bound cytochrome are also induced on admixture of dioleoylglycerol or dioleoylphosphatidylcholine with dioleoylphosphatidylglycerol. In the case of dioleoylglycerol, significant changes take place even at levels as low as 5 mol %. Binding of cytochrome c induces or increases the content of near isotropically diffusing lipid registered by the 31P NMR spectra of the different lipids studied. Admixture of dioleoylglycerol also increases the bilayer curvature of dioleoylphosphatidylglycerol, inducing an inverted hexagonal phase at 50 mol % concentration; the tendency to spontaneous curvature in the lipid appears to relax the conformational change detected in the protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9084-9
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Cytochrome c-lipid interactions studied by resonance Raman and 31P NMR spectroscopy. Correlation between the conformational changes of the protein and the lipid bilayer.
pubmed:affiliation
Max-Planck-Institut für biophysikalische Chemie, Abteilung Spektroskopie, Göttingen, Federal Republic of Germany.
pubmed:publicationType
Journal Article