TransFold: a web server for predicting the structure and residue contacts of transmembrane beta-barrels.

ABSTRACT: Transmembrane beta-barrel (TMB) proteins are embedded in the outer membrane of Gram-negative bacteria, mitochondria and chloroplasts. The cellular location and functional diversity of beta-barrel outer membrane proteins makes them an important protein class. At the present time, very few non-homologous TMB structures have been determined by X-ray diffraction because of the experimental difficulty encountered in crystallizing transmembrane (TM) proteins. The transFold web server uses pairwise inter-strand residue statistical potentials derived from globular (non-outer-membrane) proteins to predict the supersecondary structure of TMB. Unlike all previous approaches, transFold does not use machine learning methods such as hidden Markov models or neural networks; instead, transFold employs mul

SUBMITTER: Waldispuhl J 

PROVIDER: S-EPMC1538872 | biostudies-literature | 2006 Jul

REPOSITORIES: biostudies-literature