Cross-correlated chemical shift modulation: A signature of slow internal motions in proteins

D. Früh, J. R. Tolman, G. Bodenhausen, C. Zwahlen

Research output: Contribution to journalArticlepeer-review

Abstract

A novel NMR experiment allows one to characterize slow motion in macromolecules. The method exploits the fact that motions, such as rotation about dihedral angles, induce correlated fluctuations of the isotropic chemical shifts of the nuclei in the vicinity. The relaxation of two-spin coherences involving Cα and Cβ nuclei in proteins provides information about correlated fluctuations of the isotropic chemical shifts of Cα and Cβ. The difference between the relaxation rates of double- and zero-quantum coherences C+α C+β and C+α C-β is shown to be affected by cross-correlated chemical shift modulation. In ubiquitin, evidence for slow motion is found in loops or near the ends of β-strands and α-helices.

Original languageEnglish (US)
Pages (from-to)4810-4816
Number of pages7
JournalJournal of the American Chemical Society
Volume123
Issue number20
DOIs
StatePublished - Oct 6 2001
Externally publishedYes

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Fingerprint Dive into the research topics of 'Cross-correlated chemical shift modulation: A signature of slow internal motions in proteins'. Together they form a unique fingerprint.

Cite this