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Transmembrane helices of membrane proteins may flex to satisfy hydrophobic mismatch.

Abstract:

A novel mechanism for membrane modulation of transmembrane protein structure, and consequently function, is suggested in which mismatch between the hydrophobic surface of the protein and the hydrophobic interior of the lipid bilayer induces a flexing or bending of a transmembrane segment of the protein. Studies on model hydrophobic transmembrane peptides predict that helices tilt to submerge the hydrophobic surface within the lipid bilayer to satisfy the hydrophobic effect if the helix length...

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Publication status:
Published

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Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
Journal:
Biochimica et biophysica acta
Volume:
1768
Issue:
3
Pages:
530-537
Publication date:
2007-03-01
DOI:
ISSN:
0006-3002
Source identifiers:
100794

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