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Solid‐state NMR investigations of interaction contributions that determine the alignment of helical polypeptides in biological membranes
Author(s) -
Bechinger Burkhard
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02741-7
Subject(s) - chemistry , lipid bilayer , peptide , membrane , amphiphile , nuclear magnetic resonance spectroscopy , transmembrane protein , phospholipid , crystallography , solid state nuclear magnetic resonance , bilayer , biophysics , stereochemistry , biochemistry , organic chemistry , nuclear magnetic resonance , biology , receptor , copolymer , polymer , physics
Helical peptides reconstituted into oriented phospholipid bilayers were studied by proton‐decoupled 15 N solid‐state NMR spectroscopy. Whereas hydrophobic channel peptides, such as the N‐terminal region of Vpu of HIV‐1, adopt transmembrane orientations, amphipathic peptide antibiotics are oriented parallel to the bilayer surface. The interaction contributions that determine the alignment of helical peptides in lipid membranes were analysed using model sequences, and peptides that change their topology in a pH‐dependent manner have been designed. The energy contributions of histidines, lysines, leucines and alanines as well as the alignment of peptides and phospholipids under conditions of hydrophobic mismatch have been investigated in considerable detail.