Helical membrane protein folding, stability, and evolution.
Helical membrane protein folding and oligomerization can be usefully conceptualized as involving two energetically distinct stages-the formation and subsequent side-to-side association of independently stable transbilayer helices. The interactions of helices with the bilayer, with prosthetic groups, and with each other are examined in the context of recent evidence. We conclude that the two-stage concept remains useful as an approach to simplifying discussions of stability, as a framework for folding concepts, and as a basis for understanding membrane protein evolution.
Popot
J L
JL
Laboratoire de Physicochimie Moléculaire des Membranes Biologiques, Centre National de la Recherche Scientifique UPR 9052, Institut de Biologie Physico-Chimique, F-75005 Paris, France. jean-luc.popot@ibpc.fr
Engelman
D M
DM
D000818:Animals; D004355:Drug Stability; D019143:Evolution, Molecular; D006801:Humans; D008051:Lipid Bilayers / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics; D008958:Models, Molecular; D017510:Protein Folding; D017433:Protein Structure, Secondary
D008051:Lipid Bilayers; D008565:Membrane Proteins