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- W2093313385 abstract "Current solution NMR experiments for characterizing conformational exchange processes in large proteins are limited to exchange rates ca. 500-3000 s-1. A TROSY-based constant relaxation time (R1rho - R1) experiment is designed to extend this capability to measure motion with rates up to 105 s-1 in large macromolecules. The experiment combines off-resonance spin-lock rf fields, which provide access to the faster time-scale dynamics, with TROSY coherence selection, which extends the molecular-weight range available for study. When implemented on the 53-kDa dimeric enzyme triosephosphate isomerase, the experiment yielded substantial gains in signal-to-noise (up to 60%) over current experiments at modest static magnetic fields (14.1 T). The TROSY (R1rho - R1) experiment should therefore be of general utility for investigation of fast conformational exchange events in large proteins." @default.
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- W2093313385 date "2003-09-11" @default.
- W2093313385 modified "2023-09-27" @default.
- W2093313385 title "Off-Resonance TROSY (R1ρ − R1) for Quantitation of Fast Exchange Processes in Large Proteins" @default.
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- W2093313385 doi "https://doi.org/10.1021/ja037101s" @default.
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