TY - JOUR
T1 - High-Resolution NMR Determination of the Dynamic Structure of Membrane Proteins
AU - Jaremko, Mariusz
AU - Jaremko, Lukasz
AU - Villinger, Saskia
AU - Schmidt, Christian D.
AU - Griesinger, Christian
AU - Becker, Stefan
AU - Zweckstetter, Markus
PY - 2016/1/1
Y1 - 2016/1/1
N2 - 15N 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.
AB - 15N 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.
KW - NMR spectroscopy
KW - membrane proteins
KW - protein dynamics
KW - relaxation
KW - structure determination
UR - http://www.scopus.com/inward/record.url?scp=84979697086&partnerID=8YFLogxK
U2 - 10.1002/anie.201602639
DO - 10.1002/anie.201602639
M3 - Article
AN - SCOPUS:84979697086
VL - 55
SP - 10518
EP - 10521
JO - Angewandte Chemie International Edition in English
JF - Angewandte Chemie International Edition in English
SN - 1433-7851
IS - 35
ER -