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Divided-Evolution-Based Pulse Scheme for Quantifying Exchange Processes in Proteins: Powerful Complement to Relaxation Dispersion Experiments

被引：12
作者：
Bouvignies, Guillaume
Hansen, D. Flemming
Vallurupalli, Pramodh
Kay, Lewis E.
机构：
[1] Univ Toronto, Dept Biochem, Toronto, ON M5S 1A8, Canada
[2] Univ Toronto, Dept Chem, Toronto, ON M5S 1A8, Canada
[3] Univ Toronto, Dept Mol Genet, Toronto, ON M5S 1A8, Canada
来源：
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2011年 / 133卷 / 06期
基金：
加拿大健康研究院;
关键词：
CHARACTERIZING CHEMICAL-EXCHANGE; TIME-SCALE DYNAMICS; INVISIBLE EXCITED-STATES; NMR-SPECTROSCOPY; BIOLOGICAL MACROMOLECULES; SHIFTS; RESOLUTION; COUPLINGS; CATALYSIS; SEQUENCE;
D O I：
10.1021/ja109589y
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
A method for quantifying millisecond time scale exchange in proteins is presented based on scaling the rate of chemical exchange using a 2D (15)N, (1)H(N) experiment in which (15)N dwell times are separated by short spin-echo pulse trains. Unlike the popular Carr-Purcell-Meiboom-Gill (CPMG) experiment where the effects of a radio frequency field on measured transverse relaxation rates are quantified, the new approach measures peak positions in spectra that shift as the effective exchange time regime is varied. The utility of the method is established through an analysis of data recorded on an exchanging protein-ligand system for which the exchange parameters have been accurately determined using alternative approaches. Computations establish that a combined analysis of CPMG and peak shift profiles extends the time scale that can be studied to include exchanging systems with highly skewed populations and exchange rates as slow as 20 s(-1).
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收藏
页码：1935 / 1945
页数：11
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