Addressing the overlap problem in the quantitative analysis of two dimensional NMR spectra: application to (15)N relaxation measurements.
A quantitative analysis of 2D (1)H-(15)N spectra is often complicated by resonance overlap. Here a simple method is presented for resolving overlapped correlations by recording 2D projection planes from HNCO data sets. Applications are presented involving the measurement of (15)N T(1rho) relaxation rates in a high molecular weight protein, malate synthase G, and in a system that exchanges between folded and unfolded states, the drkN SH3 domain. By supplementing relaxation data recorded in the conventional way as a series of 2D (1)H-(15)N data sets with a series of a pair of projection planes the number of dynamics probes is increased significantly for both systems studied.
Tugarinov
Vitali
V
Protein Engineering Network Centres of Excellence and the Departments of Medical Genetics, Biochemistry and Chemistry, University of Toronto, M5S lA8, Toronto, Ontario, Canada.
Choy
Wing-Yiu
WY
Kupce
Eriks
E
Kay
Lewis E
LE
D000465:Algorithms; D000818:Animals; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008292:Malate Synthase / Q000737:chemistry*; D008958:Models, Molecular; D009010:Monte Carlo Method; D009587:Nitrogen Isotopes / Q000737:chemistry; D011487:Protein Conformation; D017510:Protein Folding; D018909:src Homology Domains / Q000502:physiology*
D009587:Nitrogen Isotopes; D008292:Malate Synthase