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Helix‐bundle membrane protein fold templates
Author(s) -
Bowie James U.
Publication year - 1999
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.8.12.2711
Subject(s) - fold (higher order function) , template , helix bundle , protein structure , protein design , protein folding , helix (gastropod) , membrane protein , chemistry , crystallography , biophysics , protein structure prediction , membrane , biology , biochemistry , computer science , materials science , nanotechnology , ecology , snail , programming language
Abstract In the fold recognition approach to structure prediction, a sequence is tested for compatibility with an already known fold. For membrane proteins, however, few folds have been determined experimentally. Here the feasibility of computing the vast majority of likely membrane protein folds is tested. The results indicate that conformation space can be effectively sampled for small numbers of helices. The vast majority of potential monomeric membrane protein structures can be represented by about 30‐folds for three helices, but increases exponentially to about 1, 500, 000 folds for seven helices. The generated folds could serve as templates for fold recognition or as starting points for conformational searches that are well distributed throughout conformation space.