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Specificity and promiscuity in membrane helix interactions

Published online by Cambridge University Press:  17 March 2009

Mark A. Lemmon  and
Donald M. Engelman
Mark A. Lemmon
Affiliation:
Department of Pharmacology, New York University Medical Center, 550 First Avenue, New York, NY 10016, USA
Donald M. Engelman
Affiliation:
Department of Molecular Biophysics & Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06520, USA
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Extract

The membrane-spanning portions of many integral membrane proteins consist of one or a number of transmembrane α-helices, which are expected to be independently stable on thermodynamic grounds. Side-by-side interactions between these transmembrane α-helices are important in the folding and assembly of such integral membrane proteins and their complexes. In considering the contribution of these helix–helix interactions to membrane protein folding and oligomerization, a distinction between the energetics and specificity should be recognized. A number of contributions to the energetics of transmembrane helix association within the lipid bilayer will be relatively non-specific, including those resulting from charge–charge interactions and lipid–packing effects. Specificity (and part of the energy) in transmembrane α-helix association, however, appears to rely mainly upon a detailed stereochemical fit between sets of dynamically accessible states of particular helices. In some cases, these interactions are mediated in part by prosthetic groups.

Type
Research Article
Information
Quarterly Reviews of Biophysics , Volume 27 , Issue 2 , May 1994 , pp. 157 - 218
Copyright
Copyright © Cambridge University Press 1994

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