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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2017-07-27
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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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Wu, Qinglin, Benjamin A Fenton, Jessica L Wojtaszek and Pei Zhou (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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Pei Zhou
The Zhou lab focuses on the elucidation of the structure and dynamics of protein–protein and protein–ligand interactions and their functions in various cellular processes. Our current efforts are directed at enzymes and protein complexes involved in bacterial membrane biosynthesis, translesion DNA synthesis, co-transcriptional regulation, and host-pathogen interactions. Our investigations of these important cellular machineries have led to the development of novel antibiotics and cancer therapeutics, as well as the establishment of new biotechnology adventures.
The Zhou lab integrates a variety of biochemical and biophysical tools, including NMR, X-ray crystallography, cryo-EM, and enzymology. The lab has played a major role in the development and application of innovative NMR technologies, including high-resolution, high-dimensional spectral reconstruction techniques.
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