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Melittin bound to dodecylphosphocholine micelles 1H-NMR assignments and global conformational features
Authors:Larry R Brown  Kurt Wüthrich
Institution:Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule, ETH-Hönggerberg, CH-8093 Zürich Switzerland
Abstract:Assignments have been obtained for most of the 1H-NMR lines of melittin bound to fully deuterated dodecylphosphocholine micelles by combined use of two-dimensional spin echo correlated spectroscopy and one-dimensional NMR methods. Nuclear Overhauser enhancement measurements showed that the mobility of the entire polypeptide chain is reduced by binding of melittin to the detergent micelle and that the amino-terminal and carboxy-terminal halves of the primary structure constitute separate, compact domains within the conformation of micelle-bound melittin. p2H titration experiments showed that the presence of positive charges on the four amino groups of melittin had little influence on the conformation of the micelle-bound polypeptide. Titration of tetrameric melittin with detergent provided evidence that melittin assumes similar conformations as a self-aggregated tetramer and as a monomer bound to micelles.
Keywords:Melittin  Protein-lipid interaction  Dodecylphosphocholine micelle  SECSY  spin echo correlated spectroscopy (two-dimensional)
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