Please use this identifier to cite or link to this item:
|Title:||Accurately probing slow motions on millisecond timescales with a robust NMR relaxation experiment||Authors:||Long, D.
|Issue Date:||27-Feb-2008||Citation:||Long, D., Liu, M., Yang, D. (2008-02-27). Accurately probing slow motions on millisecond timescales with a robust NMR relaxation experiment. Journal of the American Chemical Society 130 (8) : 2432-2433. ScholarBank@NUS Repository. https://doi.org/10.1021/ja710477h||Abstract:||A new pulse scheme is proposed for the accurate measurement of relaxation dispersion, which cycles the phases of CPMG pulses. Numerical simulations show that systematic errors in the measured relaxation rates mainly result from off-resonance and radio frequency inhomogeneity effects and they can be significantly suppressed with the method proposed here. The method has been demonstrated on human liver fatty acid binding protein. It allows the reliable identification of residues undergoing conformational exchange on millisecond timescales and accurate extraction of kinetics parameters. The relaxation dispersion data indicate that human liver fatty acid binding protein is highly flexible on millisecond timescales. Copyright © 2008 American Chemical Society.||Source Title:||Journal of the American Chemical Society||URI:||http://scholarbank.nus.edu.sg/handle/10635/99999||ISSN:||00027863||DOI:||10.1021/ja710477h|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.