Electrostatic and hydrophobic contributions to the folding mechanism of apocytochrome c driven by the interaction with lipid.

Journal article

In aqueous solution, while cytochrome c is a stably folded protein with a tightly packed structure at the secondary and tertiary levels, its heme-free precursor, apocytochrome c, shows all features of a structureless random coil. However, upon interaction with phospholipid vesicles or lysophospholipid micelles, apocytochrome c undergoes a conformational transition from its random coil in solution to an alpha-helical structure on association with lipid. The driving forces of this lipid-induced...

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Authors: Rankin, SE; Watts, A; Pinheiro, T

• Publication status: Published
• Journal: Biochemistry
• Volume: 37
• Issue: 36
• Pages: 12588-12595
• Publication date: 1998-09-01
• DOI: 10.1021/bi980408x
• EISSN: 1520-4995
• ISSN: 0006-2960
• Language: English
• Keywords: Static Electricity; Cytochrome c Group; Cytochromes c; Phosphatidylglycerols; Tryptophan; Horses; Phospholipids; Spectrometry, Fluorescence; Protein Structure, Secondary; Circular Dichroism; Apoproteins; Animals; Protein Folding