Probing Transient Conformational States of Proteins by Solid-State R1ρRelaxation-Dispersion NMR Spectroscopy
نویسندگان
چکیده
منابع مشابه
Probing Transient Conformational States of Proteins by Solid-State R1ρ Relaxation-Dispersion NMR Spectroscopy**
The function of proteins depends on their ability to sample a variety of states differing in structure and free energy. Deciphering how the various thermally accessible conformations are connected, and understanding their structures and relative energies is crucial in rationalizing protein function. Many biomolecular reactions take place within microseconds to milliseconds, and this timescale i...
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Paramagnetism-based nuclear pseudocontact shifts and spin relaxation enhancements contain a wealth of information in solid-state NMR spectra about electron-nucleus distances on the ∼20 Å length scale, far beyond that normally probed through measurements of nuclear dipolar couplings. Such data are especially vital in the context of structural studies of proteins and other biological molecules th...
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ژورنال
عنوان ژورنال: Angewandte Chemie International Edition
سال: 2014
ISSN: 1433-7851
DOI: 10.1002/anie.201311275