Interplay between hydrophobicity and the positive-inside rule in determining membrane-protein topology.

ABSTRACT: The energetics of membrane-protein interactions determine protein topology and structure: hydrophobicity drives the insertion of helical segments into the membrane, and positive charges orient the protein with respect to the membrane plane according to the positive-inside rule. Until recently, however, quantifying these contributions met with difficulty, precluding systematic analysis of the energetic basis for membrane-protein topology. We recently developed the dsTβL method, which uses deep sequencing and in vitro selection of segments inserted into the bacterial plasma membrane to infer insertion-energy profiles for each amino acid residue across the membrane, and quantified the insertion contribution from hydrophobicity and the positive-inside rule. Here, we present a topology-predicti

SUBMITTER: Elazar A 

PROVIDER: S-EPMC5027447 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature