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Structure and dynamics of lipid-associated states of apocytochrome c
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UNSPECIFIED (2000) Structure and dynamics of lipid-associated states of apocytochrome c. EUROPEAN JOURNAL OF BIOCHEMISTRY, 267 (5). pp. 1390-1396. ISSN 0014-2956.
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Abstract
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 | ||||
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Subjects: | Q Science > QD Chemistry | ||||
Journal or Publication Title: | EUROPEAN JOURNAL OF BIOCHEMISTRY | ||||
Publisher: | BLACKWELL SCIENCE LTD | ||||
ISSN: | 0014-2956 | ||||
Official Date: | March 2000 | ||||
Dates: |
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Volume: | 267 | ||||
Number: | 5 | ||||
Number of Pages: | 7 | ||||
Page Range: | pp. 1390-1396 | ||||
Publication Status: | Published |
Data sourced from Thomson Reuters' Web of Knowledge
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