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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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.
Published Version (Please cite this version)10.1039/c7cc05021f
Publication InfoWu, 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.
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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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