Folding of apocytochrome c in lipid micelles: formation of alpha-helix precedes membrane insertion.

Journal article

Apocytochrome c, which in aqueous solution is largely unstructured, acquires a highly alpha-helical structure upon interaction with lipid. The alpha-helix content induced in apocytochrome c depends on the lipid system, and this folding process is driven by both electrostatic and hydrophobic lipid-protein interactions. The folding kinetic mechanism of apocytochrome c induced by zwitterionic micelles of lysophosphatidylcholine (L-PC), predominantly driven by hydrophobic lipid-protein interactio...

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Authors: Bryson, E; Rankin, SE; Carey, M; Watts, A; Pinheiro, T

• Publication status: Published
• Journal: Biochemistry
• Volume: 38
• Issue: 30
• Pages: 9758-9767
• Publication date: 1999-07-01
• DOI: 10.1021/bi990119o
• EISSN: 1520-4995
• ISSN: 0006-2960
• Language: English
• Keywords: Animals; Spectrometry, Fluorescence; Cytochrome c Group; Circular Dichroism; Apoproteins; Protein Folding; Tryptophan; Protein Structure, Secondary; Kinetics; Lysophosphatidylcholines; Binding Sites; Cytochromes c; Micelles; Lipid Bilayers; Horses