Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 342125
Title Self-association of transmembrane alpha-helices in model membranes: Importance of helix orientation and role of hydrophobic mismatch
Author(s) Sparr, E.; Ash, W.L.; Nazarov, P.V.; Rijkers, D.T.S.; Hemminga, M.A.; Tieleman, D.P.; Kilian, J.A.
Source Journal of Biological Chemistry 280 (2005)47. - ISSN 0021-9258 - p. 39324 - 39331.
DOI https://doi.org/10.1074/jbc.M502810200
Department(s) Biophysics
EPS-2
Publication type Refereed Article in a scientific journal
Publication year 2005
Keyword(s) lipid-bilayers - molecular-organization - proteins - peptides - residues - packing - environment - simulation - stability - mechanism
Abstract Interactions between transmembrane helices play a key role in almost all cellular processes involving membrane proteins. We have investigated helix-helix interactions in lipid bilayers with synthetic tryptophan-flanked peptides that mimic the membrane spanning parts of membrane proteins. The peptides were functionalized with pyrene to allow the self-association of the helices to be monitored by pyrene fluorescence and Trp-pyrene fluorescence resonance energy transfer (FRET). Specific labeling of peptides at either their N or C terminus has shown that helix-helix association occurs almost exclusively between antiparallel helices. Furthermore, computer modeling suggested that antiparallel association arises primarily from the electrostatic interactions between ¿-helix backbone atoms. We propose that such interactions may provide a force for the preferentially antiparallel association of helices in polytopic membrane proteins. Helix-helix association was also found to depend on the lipid environment. In bilayers of dioleoylphosphatidylcholine, in which the hydrophobic length of the peptides approximately matched the bilayer thickness, association between the helices was found to require peptide/lipid ratios exceeding 1/25. Self-association of the helices was promoted by either increasing or decreasing the bilayer thickness, and by adding cholesterol. These results indicate that helix-helix association in membrane proteins can be promoted by unfavorable protein-lipid interactions.
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