When approaching physiological conditions, solvent exchange of amide protons in intrinsically disordered proteins (IDPs) is so pronounced that it becomes a key feature to be considered in NMR experiment design. 13 C NMR experiments recover information that is not accessible through amide proton detection, and solvent exchange can be used to increase sensitivity.
NMR Spectroscopic Studies of Intrinsically Disordered Proteins at Near-Physiological Conditions / Sergio Gil; Tomas Hosek; Zsofia Solyom; Rainer Kuemmerle; Bernhard Brutscher; Roberta Pierattelli; Isabella C. Felli. - In: ANGEWANDTE CHEMIE. INTERNATIONAL EDITION. - ISSN 1433-7851. - STAMPA. - 52:(2013), pp. 11808-11812. [10.1002/anie.201304272]
NMR Spectroscopic Studies of Intrinsically Disordered Proteins at Near-Physiological Conditions
HOSEK, TOMAS;PIERATTELLI, ROBERTA;FELLI, ISABELLA CATERINA
2013
Abstract
When approaching physiological conditions, solvent exchange of amide protons in intrinsically disordered proteins (IDPs) is so pronounced that it becomes a key feature to be considered in NMR experiment design. 13 C NMR experiments recover information that is not accessible through amide proton detection, and solvent exchange can be used to increase sensitivity.
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