Premium
Direct Measurement of Dynamic Frequency Shift Induced by Cross‐Correlations in 15 N‐Enriched Proteins
Author(s) -
Desvaux Hervé,
Kümmerle Rainer,
Kowalewski Jozef,
Luchinat Claudio,
Bertini Ivano
Publication year - 2004
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.200301034
Subject(s) - frequency shift , chemistry , anisotropy , magnetization transfer , dipole , nuclear magnetic resonance , proton , magnetization , nuclear magnetic resonance spectroscopy , molecular dynamics , molecular physics , analytical chemistry (journal) , physics , computational chemistry , optics , medicine , quantum mechanics , chromatography , radiology , organic chemistry , magnetic field , magnetic resonance imaging
We describe a new NMR experimental scheme that allows the direct determination of the dynamic frequency shift induced by chemical shift anisotropy/dipolar interaction (CSA/DD) cross‐correlations in 15 N‐enriched proteins. Its principle consists of comparing two rates of polarisation transfer between the amide proton and nitrogen. The first rate, which is independent of the dynamic frequency shift, is based on a selective Hartmann–Hahn coherence transfer. The second rate, which depends on the dynamic frequency shift, is based on a free evolution of the transverse magnetisation. We report experimental validation of this approach by measuring the average dynamic frequency shift due to CSA/DD cross‐correlations in the calcium‐binding protein D 9k . The method may also be applicable to the measurement of dynamic frequency shift induced by cross‐correlations between the Curie spin and dipolar interactions.