Premium
Direct measurement of the transverse and longitudinal 15 N chemical shift anisotropy–dipolar cross‐correlation rate constants using 1 H‐coupled HSQC spectra
Author(s) -
Hall Jennifer B.,
Fushman David
Publication year - 2003
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.1253
Subject(s) - heteronuclear single quantum coherence spectroscopy , chemistry , anisotropy , spectral line , dipole , time domain , nmr spectra database , transverse plane , nuclear magnetic resonance , two dimensional nuclear magnetic resonance spectroscopy , analytical chemistry (journal) , molecular physics , physics , optics , stereochemistry , quantum mechanics , organic chemistry , structural engineering , chromatography , computer science , computer vision , engineering
We describe direct methods for the measurement of the transverse and longitudinal 15 N chemical shift anisotropy–dipolar cross‐correlation rates based on comparison of the 15 N doublet components observed in 1 H‐coupled 1 H– 15 N HSQC‐type spectra. This allows the determination of the cross‐correlation rates with no need for correction factors associated with other methods. The signal overlap problem of coupled HSQC spectra is addressed by using the IPAP scheme (Ottiger M, Delaglio F, Bax A. J. Magn. Reson. 1998; 131: 373). The methods proposed here use a conventional t 1 evolution period, which allows one to minimize the truncation artifacts observed in a constant‐time‐type experiment (Hall JB, Dayie K, Fushman D. J. Biomol. NMR 2003; 26: 181). Applications of these measurements to the B3 domain of protein G are discussed. Copyright © 2003 John Wiley & Sons, Ltd.