Measuring hydrogen exchange in proteins by selective water saturation in 1Hâ??15N SOFAST/BEST-type experiments: advantages and limitations
Measuring hydrogen exchange in proteins by selective water saturation in 1Hâ??15N SOFAST/BEST-type experiments: advantages and limitations
Abstract HETex-SOFAST NMR (Schanda et al. in J Biomol NMR 33:199â??211, 2006) has been proposed some years ago as a fast and sensitive method for semi-quantitative measurement of site-specific amide-water hydrogen exchange effects along the backbone of proteins. Here we extend this concept to BEST readout sequences that provide a better resolution at the expense of some loss in sensitivity. We discuss the theoretical background and implementation of the experiment, and demonstrate its performance for an intrinsically disordered protein, 2 well folded globular proteins, and a transiently populated folding intermediate state. We also provide a critical evaluation of the level of accuracy that can be obtained when extracting quantitative exchange rates from HETex NMR measurements. Source: Journal of Biomolecular NMR |
All times are GMT. The time now is 03:41 AM. |
Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2024, Jelsoft Enterprises Ltd.
Search Engine Friendly URLs by vBSEO 3.6.0
Copyright, BioNMR.com, 2003-2013