A novel experiment for the quantitative measurement of CSA(H-1(N))/CSA(N-15) cross-correlated relaxation in N-15-labeled proteins

Citation
M. Tessari et Gw. Vuister, A novel experiment for the quantitative measurement of CSA(H-1(N))/CSA(N-15) cross-correlated relaxation in N-15-labeled proteins, J BIOM NMR, 16(2), 2000, pp. 171-174
Citations number
13
Categorie Soggetti
Biochemistry & Biophysics
Journal title
JOURNAL OF BIOMOLECULAR NMR
ISSN journal
09252738 → ACNP
Volume
16
Issue
2
Year of publication
2000
Pages
171 - 174
Database
ISI
SICI code
0925-2738(200002)16:2<171:ANEFTQ>2.0.ZU;2-0
Abstract
An experiment is presented which allows for the quantitative measurement of the relaxation interference between the H-1(N) CSA and N-15 CSA interactio ns in N-15 labeled proteins. A constant-time buildup scheme is used to meas ure the differential relaxation rate, eta, between double-quantum (DQ) and zero-quantum (ZQ) H-1(N)-N-15 coherences. The CSA/CSA experiment was record ed at three different B-o field strengths. The CSA(H-1(N))/CSA(N-15) cross- correlation rate was obtained from the linear fit of the measured rate, eta , versus B-o(2) for 77 residues of the EH2 domain from mouse Eps15.