Protein conformational flexibility from structure-free analysis of NMR dipolar couplings: Quantitative and absolute determination of backbone motion in ubiquitin

Loïe Salmon, Guillaume Bouvignies, Phineus Markwick, Nils Lakomek, Scott Showalter, Da Wei Li, Korvin Walter, Christian Griesinger, Rafael Brüschweiler, Martin Blackledge

Research output: Contribution to journalArticle

70 Scopus citations

Abstract

A robust procedure for the determination of proteinbackbone motions on time scales of pico- to milliseconds directly from residual dipolar couplings has been developed that requires no additional scaling relative to external references. The results for ubiquitin (blue in graph: experimental N HN order parameters) correspond closely to the amplitude, nature, and distribution of motion found in a 400 ns molecular-dynamics trajectory of ubiquitin (red).

Original languageEnglish (US)
Pages (from-to)4154-4157
Number of pages4
JournalAngewandte Chemie - International Edition
Volume48
Issue number23
DOIs
StatePublished - May 25 2009

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)

Fingerprint Dive into the research topics of 'Protein conformational flexibility from structure-free analysis of NMR dipolar couplings: Quantitative and absolute determination of backbone motion in ubiquitin'. Together they form a unique fingerprint.

  • Cite this