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

Mariusz Jaremko; Łukasz Jaremko; Saskia Villinger; Christian D. Schmidt; Christian Griesinger; Stefan Becker; Markus Zweckstetter

doi:10.1002/anie.201602639

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

Mariusz Jaremko, Łukasz Jaremko, Saskia Villinger, Christian D. Schmidt, Christian Griesinger, Stefan Becker, Markus Zweckstetter^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

23 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	10518-10521
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	55
Issue number	35
DOIs	https://doi.org/10.1002/anie.201602639
State	Published - Aug 22 2016
Externally published	Yes

Bibliographical note

Publisher Copyright:
© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim

Keywords

NMR spectroscopy
membrane proteins
protein dynamics
relaxation
structure determination

ASJC Scopus subject areas

Catalysis
General Chemistry

Access to Document

10.1002/anie.201602639

Cite this

@article{0e0e55b358fd4f12b7503dd554efdf96,

title = "High-Resolution NMR Determination of the Dynamic Structure of Membrane Proteins",

abstract = "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.",

keywords = "NMR spectroscopy, membrane proteins, protein dynamics, relaxation, structure determination",

author = "Mariusz Jaremko and {\L}ukasz Jaremko and Saskia Villinger and Schmidt, {Christian D.} and Christian Griesinger and Stefan Becker and Markus Zweckstetter",

note = "Publisher Copyright: {\textcopyright} 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim",

year = "2016",

month = aug,

day = "22",

doi = "10.1002/anie.201602639",

language = "English (US)",

volume = "55",

pages = "10518--10521",

journal = "Angewandte Chemie - International Edition",

issn = "1433-7851",

publisher = "Wiley",

number = "35",

}

TY - JOUR

T1 - High-Resolution NMR Determination of the Dynamic Structure of Membrane Proteins

AU - Jaremko, Mariusz

AU - Jaremko, Łukasz

AU - Villinger, Saskia

AU - Schmidt, Christian D.

AU - Griesinger, Christian

AU - Becker, Stefan

AU - Zweckstetter, Markus

PY - 2016/8/22

Y1 - 2016/8/22

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

SN - 1433-7851

VL - 55

SP - 10518

EP - 10521

JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

IS - 35

ER -

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

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this