title: Toward understanding driving forces in membrane protein folding.
abstract: α-Helical membrane proteins are largely composed of nonpolar residues that are embedded in the lipid bilayer. An enigma in the folding of membrane proteins is how a polypeptide chain can be condensed into the compact folded state in the environment where the hydrophobic effect cannot strongly drive molecular interactions. Probably other forces such as van der Waals packing, hydrogen bonding, and weakly polar interactions, which are regarded less important in the folding of water-soluble proteins, should emerge. However, it is not clearly understood how those individual forces operate and how they are balanced for stabilizing membrane proteins. Studying this problem is not a trivial task mainly because of the methodological challenges in controlling the reversible folding of membrane proteins in the lipid bilayer. Overcoming the hurdles, meaningful progress has been made in the field in the last few decades. This review will focus on recent studies tackling the problem of driving forces in membrane protein folding.
authors.affiliation: Department of Chemistry and Department of Biochemistry & Molecular Biology, Michigan State University, East Lansing, MI 48824, USA. Electronic address: honghd@msu.edu.
authors.forename: Heedeok
authors.initials: H
authors.lastname: Hong
mesh_terms: D002462:Cell Membrane / Q000737:chemistry* / Q000378:metabolism; D008051:Lipid Bilayers / Q000737:chemistry* / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D017510:Protein Folding
chemical_list: D008051:Lipid Bilayers; D008565:Membrane Proteins
keywords: Aromatic–aromatic interaction; Cation–π interaction; Hydrogen bonding; Membrane protein folding; Membrane protein stability; Packing interaction; Salt–bridge