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Solution‐State NMR Spectroscopy of a Seven‐Helix Transmembrane Protein Receptor: Backbone Assignment, Secondary Structure, and Dynamics
Author(s) -
Gautier Antoine,
Kirkpatrick John P.,
Nietlispach Daniel
Publication year - 2008
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.200802783
Subject(s) - transmembrane protein , protein secondary structure , transmembrane domain , helix (gastropod) , dynamics (music) , nuclear magnetic resonance spectroscopy , chemistry , molecular dynamics , crystallography , protein dynamics , characterization (materials science) , biophysics , stereochemistry , computational chemistry , nanotechnology , physics , materials science , membrane , biochemistry , receptor , biology , ecology , snail , acoustics
Protein in motion : A solution‐state NMR study on the seven‐helix transmembrane protein pSRII (see picture) in a detergent solution focused on the sequential backbone assignment, the characterization of the secondary structure, and the backbone dynamics. The structural integrity of the protein was confirmed, and mobility in the loops (ps–ns timescale) and slower motions in the helical core (μs–ms timescale) were identified.