Site-Resolved Measurement of Microsecond-to-Millisecond Conformational-Exchange Processes in Proteins by Solid-State NMR Spectroscopy
![Thumbnail](/bitstream/handle/20.500.11850/56211/ja303591y.pdf.jpg?sequence=4&isAllowed=y)
Open access
Date
2012-09-12Type
- Journal Article
ETH Bibliography
yes
Altmetrics
Abstract
We demonstrate that conformational exchange processes in proteins on microsecond-to-millisecond time scales can be detected and quantified by solid-state NMR spectroscopy. We show two independent approaches that measure the effect of conformational exchange on transverse relaxation parameters, namely Carr–Purcell–Meiboom–Gill relaxation-dispersion experiments and measurement of differential multiple-quantum coherence decay. Long coherence lifetimes, as required for these experiments, are achieved by the use of highly deuterated samples and fast magic-angle spinning. The usefulness of the approaches is demonstrated by application to microcrystalline ubiquitin. We detect a conformational exchange process in a region of the protein for which dynamics have also been observed in solution. Interestingly, quantitative analysis of the data reveals that the exchange process is more than 1 order of magnitude slower than in solution, and this points to the impact of the crystalline environment on free energy barriers. Show more
Permanent link
https://doi.org/10.3929/ethz-b-000056211Publication status
publishedExternal links
Journal / series
Journal of the American Chemical SocietyVolume
Pages / Article No.
Publisher
American Chemical SocietyOrganisational unit
03496 - Meier, Beat H. (emeritus) / Meier, Beat H. (emeritus)
More
Show all metadata
ETH Bibliography
yes
Altmetrics