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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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
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author Jaremko, Mariusz
Jaremko, Łukasz
Villinger, Saskia
Schmidt, Christian D.
Griesinger, Christian
Becker, Stefan
Zweckstetter, Markus
author_facet Jaremko, Mariusz
Jaremko, Łukasz
Villinger, Saskia
Schmidt, Christian D.
Griesinger, Christian
Becker, Stefan
Zweckstetter, Markus
author_sort Jaremko, Mariusz
collection PubMed
description (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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spelling pubmed-52164452017-01-18 High‐Resolution NMR Determination of the Dynamic Structure of Membrane Proteins Jaremko, Mariusz Jaremko, Łukasz Villinger, Saskia Schmidt, Christian D. Griesinger, Christian Becker, Stefan Zweckstetter, Markus Angew Chem Int Ed Engl Communications (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. John Wiley and Sons Inc. 2016-07-27 2016-08-22 /pmc/articles/PMC5216445/ /pubmed/27461260 http://dx.doi.org/10.1002/anie.201602639 Text en © 2016 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the Creative Commons Attribution‐NonCommercial‐NoDerivs (http://creativecommons.org/licenses/by-nc-nd/4.0/) License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made.
spellingShingle Communications
Jaremko, Mariusz
Jaremko, Łukasz
Villinger, Saskia
Schmidt, Christian D.
Griesinger, Christian
Becker, Stefan
Zweckstetter, Markus
High‐Resolution NMR Determination of the Dynamic Structure of Membrane Proteins
title High‐Resolution NMR Determination of the Dynamic Structure of Membrane Proteins
title_full High‐Resolution NMR Determination of the Dynamic Structure of Membrane Proteins
title_fullStr High‐Resolution NMR Determination of the Dynamic Structure of Membrane Proteins
title_full_unstemmed High‐Resolution NMR Determination of the Dynamic Structure of Membrane Proteins
title_short High‐Resolution NMR Determination of the Dynamic Structure of Membrane Proteins
title_sort high‐resolution nmr determination of the dynamic structure of membrane proteins
topic Communications
url 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
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