Helix-bundle membrane protein fold templates.
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.
Bowie
J U
JU
Department of Chemistry and Biochemistry and DOE Laboratory of Structural Biology and Molecular Medicine, UCLA, Los Angeles, California 90095-1570, USA. bowie@mbi.ucla.edu
D000465:Algorithms; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D017510:Protein Folding; D017433:Protein Structure, Secondary
D008565:Membrane Proteins