Ontology highlight
ABSTRACT:
SUBMITTER: Ojemalm K
PROVIDER: S-EPMC3553544 | biostudies-literature | 2012 Feb
REPOSITORIES: biostudies-literature
Molecular cell 20120125 4
α-helical integral membrane proteins critically depend on the correct insertion of their transmembrane α helices into the lipid bilayer for proper folding, yet a surprisingly large fraction of the transmembrane α helices in multispanning integral membrane proteins are not sufficiently hydrophobic to insert into the target membrane by themselves. How can such marginally hydrophobic segments nevertheless form transmembrane helices in the folded structure? Here, we show that a transmembrane helix w ...[more]