| Literature DB >> 15999419 |
Ursula Lehnert1, Yu Xia, Thomas E Royce, Chem-Sing Goh, Yang Liu, Alessandro Senes, Haiyuan Yu, Zhao Lei Zhang, Donald M Engelman, Mark Gerstein.
Abstract
We review recent computational advances in the study of membrane proteins, focusing on those that have at least one transmembrane helix. Transmembrane protein regions are, in many respects, easier to investigate computationally than experimentally, due to the uniformity of their structure and interactions (e.g. consisting predominately of nearly parallel helices packed together) on one hand and presenting the challenges of solubility on the other. We present the progress made on identifying and classifying membrane proteins into families, predicting their structure from amino-acid sequence patterns (using many different methods), and analyzing their interactions and packing The total result of this work allows us for the first time to begin to think about the membrane protein interactome, the set of all interactions between distinct transmembrane helices in the lipid bilayer.Entities:
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Year: 2004 PMID: 15999419 DOI: 10.1017/s003358350400397x
Source DB: PubMed Journal: Q Rev Biophys ISSN: 0033-5835 Impact factor: 5.318