MPRAP: an accessibility predictor for a-helical transmembrane proteins that performs well inside and outside the membrane.

ABSTRACT:

Background

In water-soluble proteins it is energetically favorable to bury hydrophobic residues and to expose polar and charged residues. In contrast to water soluble proteins, transmembrane proteins face three distinct environments; a hydrophobic lipid environment inside the membrane, a hydrophilic water environment outside the membrane and an interface region rich in phospholipid head-groups. Therefore, it is energetically favorable for transmembrane proteins to expose different types of residues in the different regions.

Results

Investigations of a set of structurally determined transmembrane proteins showed that the composition of solvent exposed residues differs significantly inside and outside the membrane. In contrast, residues buried within the interior of a protein

SUBMITTER: Illergard K 

PROVIDER: S-EPMC2904353 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature