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Unfolding and refolding of cytochrome c driven by the interaction with lipid micelles
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UNSPECIFIED. (2000) Unfolding and refolding of cytochrome c driven by the interaction with lipid micelles. PROTEIN SCIENCE, 9 (6). pp. 1194-1202. ISSN 0961-8368
Full text not available from this repository.Abstract
Binding of native cyt c to L-PG micelles leads to a partially unfolded conformation of cyt c. This micelle-bound state has no stable tertiary structure. but remains as cu-helical as native cvt c in solution. In contrast, binding of the acid-unfolded cvt c to L-PG micelles induces folding of the polypeptide. resulting in a similar helical state to that originated from the binding of native cyt c to L-PG micelles. Far-ultraviolet (UV) circular dichroism (CD) spectra showed that this common micelle-associated helical state (H-L) has a native-like alpha-helix content, but is highly expanded without a tightly packed hydrophobic core, as revealed by tryptophan fluorescence, near-UV, and Sent CD spectroscopy. The kinetics of the interaction of native and acid-unfolded cyt c was investigated by stopped-flow tryptophan fluorescence. Formation of HL from the native state requires the disruption of the tightly packed hydrophobic core in the native protein. This micelle-induced unfolding of cyt c occurs at a rate similar to 0.1 s(-1), which is remarkably faster in the lipid environment compared with the expected rate of unfolding in solution. Refolding of acid-unfolded cyt c with L-PG micelles involves an early highly helical collapsed state formed during the burst phase (<3 ms), and the observed main kinetic event reports on the opening of this early compact intermediate prior to insertion into the lipid micelle.
| Item Type: | Journal Article |
|---|---|
| Subjects: | Q Science > QD Chemistry |
| Journal or Publication Title: | PROTEIN SCIENCE |
| Publisher: | CAMBRIDGE UNIV PRESS |
| ISSN: | 0961-8368 |
| Date: | June 2000 |
| Volume: | 9 |
| Number: | 6 |
| Number of Pages: | 9 |
| Page Range: | pp. 1194-1202 |
| Publication Status: | Published |
| URI: | http://wrap.warwick.ac.uk/id/eprint/13254 |
Data sourced from Thomson Reuters' Web of Knowledge
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