Structure and dynamics of lipid-associated states of apocytochrome c
UNSPECIFIED. (2000) Structure and dynamics of lipid-associated states of apocytochrome c. EUROPEAN JOURNAL OF BIOCHEMISTRY, 267 (5). pp. 1390-1396. ISSN 0014-2956Full text not available from this repository.
Apocytochrome c (apocyt c), which in aqueous solution is largely unstructured, acquires an alpha-helical conformation upon association with lipid membranes. The extent of alpha-helix induced in apocyt c is lipid-dependent and this folding process is driven by both electrostatic and hydrophobic lipid-protein interactions. The structural and dynamic properties of apocyt c in lipid membranes were investigated by attenuated total reflection Fourier transform infrared spectroscopy combined with amide H-D exchange kinetics. Apocyt c acquires a higher content of alpha-helical structure with negatively charged membranes than with zwitterionic ones. For all membranes studied here, the helices of these partially folded states of apocyt c have a preferential orientation perpendicular to the plane of the lipid membrane. The H-D exchange revealed that a small fraction of amide protons of apocyt c, possibly associated with a stable folded domain protected by the lipid, remained protected from exchange over 20 min. However, a large fraction of amide protons exchanged in less than 20 min, indicating that the helical states of apocyt c in lipid membranes are very dynamic.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry|
|Journal or Publication Title:||EUROPEAN JOURNAL OF BIOCHEMISTRY|
|Publisher:||BLACKWELL SCIENCE LTD|
|Official Date:||March 2000|
|Number of Pages:||7|
|Page Range:||pp. 1390-1396|
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