A strategy for modelling transmembrane alpha-helix bundles has been investigated. Results concerning the rotational orientations of the helices are described and perspectives for extensions of the method are discussed. alpha-Helix bundles are expectedto be a common structural organisation scheme of the transmembrane region of many integral proteins. The impossibility of establishing hydrogen bonds between protein segments of the hydrocarbon chains of the lipids induces membrane proteins to stabilizethemselves by internal hydrogen bonding.
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