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Structure and dynamics of lipid-associated states of apocytochrome c
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UNSPECIFIED (2000) Structure and dynamics of lipid-associated states of apocytochrome c. EUROPEAN JOURNAL OF BIOCHEMISTRY, 267 (5). pp. 1390-1396. ISSN 0014-2956
Full text not available from this repository.Abstract
Apocytochrome c (apocyt c), which in aqueous solution is largely unstructured, acquires an alpha-helical conformation upon association with lipid membranes. The extent of alpha-helix induced in apocyt c is lipid-dependent and this folding process is driven by both electrostatic and hydrophobic lipid-protein interactions. The structural and dynamic properties of apocyt c in lipid membranes were investigated by attenuated total reflection Fourier transform infrared spectroscopy combined with amide H-D exchange kinetics. Apocyt c acquires a higher content of alpha-helical structure with negatively charged membranes than with zwitterionic ones. For all membranes studied here, the helices of these partially folded states of apocyt c have a preferential orientation perpendicular to the plane of the lipid membrane. The H-D exchange revealed that a small fraction of amide protons of apocyt c, possibly associated with a stable folded domain protected by the lipid, remained protected from exchange over 20 min. However, a large fraction of amide protons exchanged in less than 20 min, indicating that the helical states of apocyt c in lipid membranes are very dynamic.
| Item Type: | Journal Article |
|---|---|
| Subjects: | Q Science > QD Chemistry |
| Journal or Publication Title: | EUROPEAN JOURNAL OF BIOCHEMISTRY |
| Publisher: | BLACKWELL SCIENCE LTD |
| ISSN: | 0014-2956 |
| Date: | March 2000 |
| Volume: | 267 |
| Number: | 5 |
| Number of Pages: | 7 |
| Page Range: | pp. 1390-1396 |
| Publication Status: | Published |
| URI: | http://wrap.warwick.ac.uk/id/eprint/13522 |
Data sourced from Thomson Reuters' Web of Knowledge
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