High-Resolution NMR Determination of the Dynamic Structure of Membrane Proteins.

Authors :: Jaremko M
Jaremko Ł
Villinger S
Schmidt CD
Griesinger C
Becker S
Zweckstetter M
Source :: Angewandte Chemie (International ed. in English) [Angew Chem Int Ed Engl] 2016 Aug 22; Vol. 55 (35), pp. 10518-21. Date of Electronic Publication: 2016 Jul 27.
Publication Year :: 2016
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.<br /> (© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)

Subjects :: Humans
Protein Conformation
Membrane Proteins chemistry
Molecular Dynamics Simulation
Nuclear Magnetic Resonance, Biomolecular

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