Molecular Motions:<i>T</i><sub>1</sub>Frequency Dispersion in Biological Systems

Kimmich, Rainer

doi:10.1002/9780470034590.emrstm0314

Cited by 1 publication

(1 citation statement)

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“…Ironically, this high-field regime is not as sensitive to mesodynamics as relaxation data at lower fields. Low-field R 1 relaxation experiments covering 1 H Larmor frequencies up to several tens of MHz have been performed using field-cycling relaxometers (Kimmich 1996 ; Luchinat and Parigi 2007 ). Due to the low resolution, these experiments have usually probed the relaxation of solvent protons as reporters, and are therefore limited.…”

Section: Introductionmentioning

confidence: 99%

Mesodynamics in the SARS nucleocapsid measured by NMR field cycling

et al. 2009

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Protein motions on all timescales faster than molecular tumbling are encoded in the spectral density. The dissection of complex protein dynamics is typically performed using relaxation rates determined at high and ultrahigh field. Here we expand this range of the spectral density to low fields through field cycling using the nucleocapsid protein of the SARS coronavirus as a model system. The field-cycling approach enables site-specific measurements of R 1 at low fields with the sensitivity and resolution of a high-field magnet. These data, together with high-field relaxation and heteronuclear NOE, provide evidence for correlated rigid-body motions of the entire b-hairpin, and corresponding motions of adjacent loops with a time constant of 0.8 ns (mesodynamics). MD simulations substantiate these findings and provide direct verification of the time scale and collective nature of these motions.

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Section: Introductionmentioning

confidence: 99%