Modeling membrane proteins utilizing information from silent amino acid substitutions.

Uzi Kochva*, Hadas Leonov, Isaiah T. Arkin, Paul D. Adams

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

This unit describes predicting the structure of simple transmembrane alpha-helical bundles. The protocol is based on a global molecular dynamics search (GMDS) of the configuration space of the helical bundle, yielding several candidates structures. The correct structure amongst these candidates is selected using information from silent amino acid substitutions, employing the following premise: Only the correct structure must (by definition) accept all of the silent amino acid substitutions. Thus, the correct structure is found by repeating the GMDS for several close homologues and selecting the structure that persists in all of the trials.

Original languageAmerican English
Pages (from-to)Unit5.3
JournalCurrent Protocols in Bioinformatics
VolumeChapter 5
StatePublished - Feb 2004

Fingerprint

Dive into the research topics of 'Modeling membrane proteins utilizing information from silent amino acid substitutions.'. Together they form a unique fingerprint.

Cite this