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High‐Resolution NMR Determination of the Dynamic Structure of Membrane Proteins
Author(s) -
Jaremko Mariusz,
Jaremko Łukasz,
Villinger Saskia,
Schmidt Christian D.,
Griesinger Christian,
Becker Stefan,
Zweckstetter Markus
Publication year - 2016
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201602639
Subject(s) - chemistry , membrane protein , membrane , relaxation (psychology) , ion , resolution (logic) , nuclear magnetic resonance spectroscopy , crystallography , biophysics , analytical chemistry (journal) , stereochemistry , chromatography , biochemistry , organic chemistry , social psychology , artificial intelligence , computer science , biology , psychology
Abstract 15 N spin‐relaxation rates are demonstrated to provide critical information about the long‐range structure and internal motions of membrane proteins. Combined with an improved calculation method, the relaxation‐rate‐derived structure of the 283‐residue human voltage‐dependent anion channel revealed an anisotropically shaped barrel with a rigidly attached N‐terminal helix. Our study thus establishes an NMR spectroscopic approach to determine the structure and dynamics of mammalian membrane proteins at high accuracy and resolution.