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

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.

SUBMITTER: Jaremko M

PROVIDER: S-EPMC5216445 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature

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

Jaremko Mariusz M Jaremko Łukasz Ł Villinger Saskia S Schmidt Christian D CD Griesinger Christian C Becker Stefan S Zweckstetter Markus M

Angewandte Chemie (International ed. in English) 20160727 35

(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 prot ...[more]

PMID: 27461260

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