How proteins adapt to a membrane-water interface.
Membrane proteins present a hydrophobic surface to the surrounding lipid, whereas portions protruding into the aqueous milieu expose a polar surface. But how have proteins evolved to deal with the complex environment at the membrane-water interface? Some insights have been provided by high-resolution structures of membrane proteins, and recent studies of the role of individual amino acids in mediating protein-lipid contacts have shed further light on this issue. It now appears clear that the polar-aromatic residues Trp and Tyr have a specific affinity for a region near the lipid carbonyls, whereas positively charged residues extend into the lipid phosphate region.
Killian
J A
JA
Dept of Biochemistry of Membranes, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands. j.a.killian@chem.uu.nl
von Heijne
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D000596:Amino Acids / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D006031:Glycosylation; D008051:Lipid Bilayers / Q000737:chemistry; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry; D017433:Protein Structure, Secondary; D014364:Tryptophan / Q000737:chemistry / Q000378:metabolism; D014443:Tyrosine / Q000737:chemistry / Q000378:metabolism; D014867:Water / Q000378:metabolism*
D000596:Amino Acids; D008051:Lipid Bilayers; D010455:Peptides; D014867:Water; D014443:Tyrosine; D014364:Tryptophan