Association of ferri- and ferro-cytochrome c with lipid multilayers: A super(31)P solid-state NMR study

The super(31)P nuclear magnetic resonance anisotropies of dispersions of diacylphosphatidic acid and diacylphosphatidylserine were slightly increased in the presence of cytochrome c: no increase was observed with cardiolipin. However, the super(31)P spin-lattice relaxation time (T sub(1)) for all of...

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Published inBiochimica et biophysica acta, Protein structure and molecular enzymology Vol. 862; no. 2; pp. 451 - 456
Main Authors Waltham, M C, Cornell, BA, Smith, R
Format Journal Article
LanguageEnglish
Published 01.01.1986
Subjects
cytochrome c
diacylphosphatidic acid
diacylphosphatidylserine
lipid bilayers
N.M.R
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Summary:The super(31)P nuclear magnetic resonance anisotropies of dispersions of diacylphosphatidic acid and diacylphosphatidylserine were slightly increased in the presence of cytochrome c: no increase was observed with cardiolipin. However, the super(31)P spin-lattice relaxation time (T sub(1)) for all of these lipids were reduced markedly by the protein. As similar effects were observed with ferri-cytochrome c and with the reduced protein, which is diamagnetic, the authors suggests that the changes in T sub(1) reflect a reduction in the spectral density of fast motions for the lipid headgroups attendant on binding of protein, rather than paramagnetic relaxation of the phosphorus nuclear spin.
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ISSN:0167-4838