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) |
本文献已被 ScienceDirect 等数据库收录! |