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Folding of apocytochrome c induced by the interaction with negatively charged lipid micelles proceeds via a collapsed intermediate state
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UNSPECIFIED (1999) Folding of apocytochrome c induced by the interaction with negatively charged lipid micelles proceeds via a collapsed intermediate state. PROTEIN SCIENCE, 8 (2). pp. 381-393. ISSN 0961-8368.
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Abstract
Unfolded apocytochrome c acquires an alpha-helical conformation upon interaction with lipid. Folding kinetic results below and above the lipid's CMC, together with energy transfer measurements of lipid bound states, and salt-induced compact states in solution, show that the folding transition of apocytochrome c from the unfolded state in solution to a lipid-inserted helical conformation proceeds via a collapsed intermediate state (I-C). This initial compact state is driven by a hydrophobic collapse of the polypeptide chain in the absence of the heme group and may represent a hems-free analogue of an early compact intermediate detected on the folding pathway of cytochrome c in solution. Insertion into the lipid phase occurs via an unfolding step of I-C through a more extended state associated with the membrane surface (I-S). While I-C appears to be as compact as salt-induced compact states in solution with substantial alpha-helix content, the final lipid-inserted state (H-mic) is as compact as the unfolded state in solution at pH 5 and has an alpha-helix content which resembles that of native cytochrome c.
Item Type: | Journal Article | ||||
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Subjects: | Q Science > QD Chemistry | ||||
Journal or Publication Title: | PROTEIN SCIENCE | ||||
Publisher: | CAMBRIDGE UNIV PRESS | ||||
ISSN: | 0961-8368 | ||||
Official Date: | February 1999 | ||||
Dates: |
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Volume: | 8 | ||||
Number: | 2 | ||||
Number of Pages: | 13 | ||||
Page Range: | pp. 381-393 | ||||
Publication Status: | Published |
Data sourced from Thomson Reuters' Web of Knowledge
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