Modest stabilization by most hydrogen-bonded side-chain interactions in membrane proteins.

ABSTRACT: Understanding the energetics of molecular interactions is fundamental to all of the central quests of structural biology including structure prediction and design, mapping evolutionary pathways, learning how mutations cause disease, drug design, and relating structure to function. Hydrogen-bonding is widely regarded as an important force in a membrane environment because of the low dielectric constant of membranes and a lack of competition from water. Indeed, polar residue substitutions are the most common disease-causing mutations in membrane proteins. Because of limited structural information and technical challenges, however, there have been few quantitative tests of hydrogen-bond strength in the context of large membrane proteins. Here we show, by using a double-mutant cycle analysis,

SUBMITTER: Joh NH 

PROVIDER: S-EPMC2734483 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature