TY - JOUR
T1 - Least-squares method for quantitative determination of chemical exchange and cross-relaxation rate constants from a series of two-dimensional exchange NMR spectra
AU - Zolnai, Zsolt
AU - Juranić, Nenad
AU - Macura, Slobodan
PY - 1997/5/15
Y1 - 1997/5/15
N2 - We present a new method, the least-error matrix analysis (LEMA), to quantify the dynamic matrix from a series of 2D NMR exchange spectra. The method is based on a weighted averaging of individual dynamic matrices. The matrices are obtained by full-matrix analysis (FMA) from a series of 2D exchange spectra recorded at different mixing times. The weights, calculated by error propagation analysis, are explicit functions of the mixing time. The principal advantage of LEMA in comparison to FMA is that it uses all the known relationships between the spectral peaks: the peak correlations within 2D spectra, and the mixing time evolution among the spectra. We tested LEMA by analyzing a series of 10 cross-relaxation spectra (NOESY, τm = 60 μs-1.28 s) in a rigid 10-spin system (cyclo(L-Pro-Gly) in 3:1 v/v H2O/DMSO). At 233 K the dipeptide has a mobility like a small protein with a correlation time of 3.8 ns. While FMA at τm = 30 ms could extract only 14 distances in a range 1.75-3 Å, LEMA provided 22 distances, of which the longest was 4 Å. The extension of the available interproton distances from 3 to 4 Å afforded by LEMA is caused by a 10-fold decrease of the lower limit of measurable cross-relaxation rates, from -0.59 to -0.06 s-1. The most important property of LEMA, provision of accurate average values of magnetization exchange rates from a given set of peak volumes, is verified experimentally on a model system.
AB - We present a new method, the least-error matrix analysis (LEMA), to quantify the dynamic matrix from a series of 2D NMR exchange spectra. The method is based on a weighted averaging of individual dynamic matrices. The matrices are obtained by full-matrix analysis (FMA) from a series of 2D exchange spectra recorded at different mixing times. The weights, calculated by error propagation analysis, are explicit functions of the mixing time. The principal advantage of LEMA in comparison to FMA is that it uses all the known relationships between the spectral peaks: the peak correlations within 2D spectra, and the mixing time evolution among the spectra. We tested LEMA by analyzing a series of 10 cross-relaxation spectra (NOESY, τm = 60 μs-1.28 s) in a rigid 10-spin system (cyclo(L-Pro-Gly) in 3:1 v/v H2O/DMSO). At 233 K the dipeptide has a mobility like a small protein with a correlation time of 3.8 ns. While FMA at τm = 30 ms could extract only 14 distances in a range 1.75-3 Å, LEMA provided 22 distances, of which the longest was 4 Å. The extension of the available interproton distances from 3 to 4 Å afforded by LEMA is caused by a 10-fold decrease of the lower limit of measurable cross-relaxation rates, from -0.59 to -0.06 s-1. The most important property of LEMA, provision of accurate average values of magnetization exchange rates from a given set of peak volumes, is verified experimentally on a model system.
UR - http://www.scopus.com/inward/record.url?scp=0013574441&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0013574441&partnerID=8YFLogxK
U2 - 10.1021/jp963956y
DO - 10.1021/jp963956y
M3 - Article
AN - SCOPUS:0013574441
SN - 1089-5639
VL - 101
SP - 3707
EP - 3710
JO - Journal of Physical Chemistry A
JF - Journal of Physical Chemistry A
IS - 20
ER -