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

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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

16 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 languageEnglish (US)
Pages (from-to)10518-10521
Number of pages4
JournalAngewandte Chemie - International Edition
Volume55
Issue number35
DOIs
StatePublished - Jan 1 2016

Keywords

  • NMR spectroscopy
  • membrane proteins
  • protein dynamics
  • relaxation
  • structure determination

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

Fingerprint

Dive into the research topics of 'High-Resolution NMR Determination of the Dynamic Structure of Membrane Proteins'. Together they form a unique fingerprint.

Cite this