High‐Resolution NMR Determination of the Dynamic Structure of Membrane Proteins

(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...

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Detalles Bibliográficos
Autores principales: Jaremko, Mariusz, Jaremko, Łukasz, Villinger, Saskia, Schmidt, Christian D., Griesinger, Christian, Becker, Stefan, Zweckstetter, Markus
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2016
Materias:
Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5216445/
https://www.ncbi.nlm.nih.gov/pubmed/27461260
http://dx.doi.org/10.1002/anie.201602639
Descripción
Sumario:(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.

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