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Probing the excited-state chemical shifts and exchange parameters by nitrogen-decoupled amide proton chemical exchange saturation transfer (HN(dec)-CEST).

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Date
2017-07-27
Authors
Wu, Qinglin
Fenton, Benjamin A
Wojtaszek, Jessica L
Zhou, Pei
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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.
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Journal article
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https://hdl.handle.net/10161/15818
Published Version (Please cite this version)
10.1039/c7cc05021f
Publication 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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Scholars@Duke

Zhou

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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