Ontology highlight
ABSTRACT:
SUBMITTER: Paslawski W
PROVIDER: S-EPMC4491732 | biostudies-literature | 2015 Jun
REPOSITORIES: biostudies-literature
Paslawski Wojciech W Lillelund Ove K OK Kristensen Julie Veje JV Schafer Nicholas P NP Baker Rosanna P RP Urban Sinisa S Otzen Daniel E DE
Proceedings of the National Academy of Sciences of the United States of America 20150608 26
Despite the ubiquity of helical membrane proteins in nature and their pharmacological importance, the mechanisms guiding their folding remain unclear. We performed kinetic folding and unfolding experiments on 69 mutants (engineered every 2-3 residues throughout the 178-residue transmembrane domain) of GlpG, a membrane-embedded rhomboid protease from Escherichia coli. The only clustering of significantly positive ϕ-values occurs at the cytosolic termini of transmembrane helices 1 and 2, which we ...[more]