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Inside Cover: Solution‐State NMR Spectroscopy of a Seven‐Helix Transmembrane Protein Receptor: Backbone Assignment, Secondary Structure, and Dynamics (Angew. Chem. Int. Ed. 38/2008)
Author(s) -
Gautier Antoine,
Kirkpatrick John P.,
Nietlispach Daniel
Publication year - 2008
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200890186
Subject(s) - cover (algebra) , chemistry , helix (gastropod) , nuclear magnetic resonance spectroscopy , transmembrane protein , spectroscopy , int , transmembrane domain , molecular dynamics , crystallography , stereochemistry , computational chemistry , receptor , physics , biochemistry , mechanical engineering , ecology , snail , engineering , biology , quantum mechanics , computer science , operating system
Untangling the structure of a helical membrane protein is intricate work. In their Communication on page 7297 ff. D. Nietlispach and co‐workers present a high‐resolution solution‐state NMR study of the seven‐helical transmembrane protein receptor sensory rhodopsin II from Natronomonas pharaonis. They discuss triple‐resonance‐based sequential assignments, secondary structure, solvent exchange, and backbone dynamics of the detergent‐solubilized protein.