[NMR paper] Microsecond dynamics in ubiquitin probed by solid-state NMR 15N R1rho relaxation experiments under fast MAS (60-110 kHz).

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Microsecond dynamics in ubiquitin probed by solid-state NMR 15N R1rho relaxation experiments under fast MAS (60-110 kHz).

Related Articles Microsecond dynamics in ubiquitin probed by solid-state NMR 15N R1rho relaxation experiments under fast MAS (60-110 kHz).

Chemistry. 2017 Apr 20;:

Authors: Lakomek NA, Penzel S, Lends A, Cadalbert R, Ernst M, Meier BH

Abstract
15N R1? relaxation experiments in solid-state NMR are sensitive to timescales and amplitudes of internal protein motions in the hundreds of ns to µs time window, difficult to probe with solution-state NMR. Using 15N R1? relaxation experiments with variable MAS frequency (60-110 kHz) and a model-free analysis, we describe an approach to detect hundreds of ns to low µs protein dynamics and determine residue-specific correlation times from the ratio of 15N R1? rate constants at different MAS frequencies. We find that microcrystalline ubiquitin exhibits small-amplitude dynamics on a timescale of about 1*µs across the entire protein, and larger amplitude motions, also on the 1*µs timescale, for several sites, including the ?1-?2 turn and the N-terminus of the ?-helix. According to our analysis, the µs protein backbone dynamics are of lower amplitude than concluded in previous NMR studies but persist across the entire protein with a rather uniform timescale of 1*µs.


PMID: 28426169 [PubMed - as supplied by publisher]



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