Probing the excited-state chemical shifts and exchange parameters by nitrogen-decoupled amide proton chemical exchange saturation transfer (HN(dec)-CEST).
Abstract
CEST-NMR spectroscopy is a powerful tool for probing the conformational dynamics of
macromolecules. We present a HN(dec)-CEST experiment that simplifies the relaxation
matrix, reduces fitting parameters, and enhances signal resolution. Importantly, fitting
of HN(dec)-CEST profiles enables robust extraction of exchange rates as well as excited-state
chemical shifts and populations.
Type
Journal articlePermalink
https://hdl.handle.net/10161/15818Published Version (Please cite this version)
10.1039/c7cc05021fPublication Info
Wu, Qinglin; Fenton, Benjamin A; Wojtaszek, Jessica L; & Zhou, Pei (2017). Probing the excited-state chemical shifts and exchange parameters by nitrogen-decoupled
amide proton chemical exchange saturation transfer (HN(dec)-CEST). Chem Commun (Camb), 53(61). pp. 8541-8544. 10.1039/c7cc05021f. Retrieved from https://hdl.handle.net/10161/15818.This is constructed from limited available data and may be imprecise. To cite this
article, please review & use the official citation provided by the journal.
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Show full item recordScholars@Duke
Pei Zhou
Professor of Biochemistry
Protein-protein interactions play a pivotal role in the regulation of various cellular
processes. The formation of higher order protein complexes is frequently accompanied
by extensive structural remodeling of the individual components, varying from domain
re-orientation to induced folding of unstructured elements. Nuclear Magnetic Resonance
(NMR) spectroscopy is a powerful tool for macromolecular structure determination in
solution. It has the unique advantage of being capable of elucidati

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