Structural and kinetic description of cytochrome c unfolding induced by the interaction with lipid vesicles.

Journal article

The interaction of cytochrome c with anionic lipid vesicles of DOPS induces an extensive disruption of the native structure of the protein. The kinetics of this lipid-induced unfolding process were investigated in a series of fluorescence- and absorbance-detected stopped-flow measurements. The results show that the tightly packed native structure of cytochrome c is disrupted at a rate of approximately 1.5 s-1 (independent of protein and lipid concentration), leading to the formation of a lipi...

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Authors: Pinheiro, T; Elöve, G; Watts, A; Roder, H

• Publication status: Published
• Journal: Biochemistry
• Volume: 36
• Issue: 42
• Pages: 13122-13132
• Publication date: 1997-10-01
• DOI: 10.1021/bi971235z
• EISSN: 1520-4995
• ISSN: 0006-2960
• Language: English
• Keywords: Protein Conformation; Liposomes; Phosphatidylserines; Binding Sites; Horses; Kinetics; Microscopy, Fluorescence; Heme; Models, Chemical; Methionine; Circular Dichroism; Spectrophotometry; Animals; Cytochrome c Group; Protein Denaturation