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Cytochrome c interactions with cardiolipin in bilayers: a multinuclear magic-angle spinning NMR study.

Abstract:

The influence of cytochrome c binding to cardiolipin bilayers on the motional characteristics of each component has been analyzed by magic-angle spinning (MAS) NMR. Observations were made by NMR of natural abundance 31P, 13C, and 1H nuclei in the lipid as well as sites enriched with 13C in the protein. Analysis of methyl carbons enriched in ([epsilon-13CH3]methionine)cytochrome c at residues 65 and 80 reveal quite different behavior for these sites when the protein was bound at a 1:15 molar r...

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Publication status:
Published

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Publisher copy:
10.1021/bi00156a037

Authors


Spooner, PJ More by this author
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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Journal:
Biochemistry
Volume:
31
Issue:
41
Pages:
10129-10138
Publication date:
1992-10-05
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
URN:
uuid:55150ace-01ab-416b-b5e0-7ac57eaaabf4
Source identifiers:
422169
Local pid:
pubs:422169

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