Folding of apocytochrome c induced by the interaction with negatively charged lipid micelles proceeds via a collapsed intermediate state
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 0961-8368Full text not available from this repository.
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|
|Subjects:||Q Science > QD Chemistry|
|Journal or Publication Title:||PROTEIN SCIENCE|
|Publisher:||CAMBRIDGE UNIV PRESS|
|Official Date:||February 1999|
|Number of Pages:||13|
|Page Range:||pp. 381-393|
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