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Abstract
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.