Microsecond timescale protein dynamics: a combined solid-state NMR approach.
Related Articles Microsecond timescale protein dynamics: a combined solid-state NMR approach.
Chemphyschem. 2017 Nov 17;:
Authors: Rovó P, Linser R
Abstract
Conformational exchange in proteins is a major determinant in protein functionality. In particular, the ?s-ms timescale is associated with enzymatic activity and interactions between biological molecules. We show here that a comprehensive data set of R1? relaxation dispersion profiles employing multiple effective fields and tilt angles can be easily obtained in perdeuterated, partly back-exchanged proteins at fast magic-angle spinning and further complemented with chemical-exchange saturation transfer NMR experiments. The approach exploits complementary sources of information and enables the extraction of multiple exchange parameters for ?s-ms timescale conformational exchange, most notably including the sign of the chemical shift differences between the ground and excited states.
PMID: 29149466 [PubMed - as supplied by publisher]
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