NDLI: Unfolding and refolding of cytochrome c driven by the interaction with lipid micelles.

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Unfolding and refolding of cytochrome c driven by the interaction with lipid micelles.

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Unfolding and refolding of cytochrome c driven by the interaction with lipid micelles.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Sanghera, N. Pinheiro, T. J.
Description	Country affiliation: United kingdom Author Affiliation: Sanghera N ( Department of Biological Sciences, University of Warwick, Coventry, United Kingdom.)
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 alpha-helical as native cyt c in solution. In contrast, binding of the acid-unfolded cyt 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 (HL) 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 Soret CD spectroscopy. The kinetics of the interaction of native and acid-unfolded cyt c was investigated by stopped-flow tryptophan fluorescence. Formation of H(L) 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 approximately 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.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	6
Volume Number	9
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2000-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cytochrome c Group Chemistry Lysophospholipids Micelles Circular Dichroism Kinetics Protein Folding Spectrometry, Fluorescence Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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