Topography prediction of helical transmembrane proteins by a new modification of the sliding window method.

ABSTRACT: Protein functions are specified by its three-dimensional structure, which is usually obtained by X-ray crystallography. Due to difficulty of handling membrane proteins experimentally to date the structure has only been determined for a very limited part of membrane proteins (<4%). Nevertheless, investigation of structure and functions of membrane proteins is important for medicine and pharmacology and, therefore, is of significant interest. Methods of computer modeling based on the data on the primary protein structure or the symbolic amino acid sequence have become an actual alternative to the experimental method of X-ray crystallography for investigating the structure of membrane proteins. Here we presented the results of the study of 35 transmembrane proteins, mainly GPCRs, using the no

SUBMITTER: Simakova MN 

PROVIDER: S-EPMC4034515 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature