An NMR experiment for the accurate measurement of heteronuclear spin-lock relaxation rates.
Rotating-frame relaxation rates, R(1)(rho), are often measured in NMR studies of protein dynamics. We show here that large systematic errors can be introduced into measured values of heteronuclear R(1)(rho) rates using schemes which are usually employed to suppress cross-correlation between dipole-dipole and CSA relaxation mechanisms. For example, in a scalar-coupled two-spin X-H spin system the use of (1)H WALTZ16 decoupling or (1)H pulses applied at regularly spaced intervals leads to a significant overestimation of heteronuclear R(1)(rho) values. The problem is studied experimentally and theoretically for (15)N-(1)H and (13)C-(1)H spin pairs, and simple schemes are described which eliminate the artifacts. The approaches suggested are essential replacements of existing methodology if accurate dynamics parameters are to be extracted from spin-lock relaxation data sets.
Protein Engineering Network Centers of Excellence and Departments of Medical Genetics, Biochemistry and Chemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada.
Dmitry M
DM
Korzhnev
Nikolai R
NR
Skrynnikov
Oscar
O
Millet
Dennis A
DA
Torchia
Lewis E
LE
Kay
D001426:Bacterial Proteins; D002247:Carbon Isotopes; D003198:Computer Simulation; D004268:DNA-Binding Proteins / Q000737:chemistry; D008956:Models, Chemical; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011506:Proteins / Q000737:chemistry*; D018909:src Homology Domains
D001426:Bacterial Proteins; D002247:Carbon Isotopes; D004268:DNA-Binding Proteins; C116593:L-protein, Peptococcus magnus; D009587:Nitrogen Isotopes; D011506:Proteins