Life at the border: adaptation of proteins to anisotropic membrane environment.

摘要: This review discusses main features of transmembrane (TM) proteins which distinguish them from water-soluble and allow their adaptation to the anisotropic membrane environment. We overview structural limitations on protein architecture, spatial arrangement in membranes intrinsic hydrophobic thickness, co-translational post-translational folding insertion into lipid bilayers, topogenesis, high propensity form oligomers, large-scale conformational transitions during transport function. Special attention is paid polarity TM surfaces described by profiles dipolarity/polarizability hydrogen-bonding capacity parameters that match Analysis distributions Trp resides different biological indicates interfacial regions with preferential accumulation indole rings correspond outer part acyl chain region—between double bonds carbonyl groups lipids. These “midpolar” are not always symmetric natural membranes. also examined effect drives bilayer free energy contributions stability, including attractive van der Waals forces hydrogen bonds, side-chain entropy, mismatch, deformations, specific protein–lipid binding.