[NMR paper] Multiple Scale Dynamics in Proteins Probed at Multiple Time Scales through Fluctuations of NMR Chemical Shifts.

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Multiple Scale Dynamics in Proteins Probed at Multiple Time Scales through Fluctuations of NMR Chemical Shifts.

Related Articles Multiple Scale Dynamics in Proteins Probed at Multiple Time Scales through Fluctuations of NMR Chemical Shifts.

J Phys Chem B. 2014 Mar 14;

Authors: Calligari PA, Abergel D

Abstract
Fluctuations of NMR resonance frequency shifts and their relation with protein exchanging conformations are usually analysed in terms of simple two-site jump processes. However, this description is unable to account for the presence of multiple time scale dynamics. In this work, we present an alternative model for the interpretation of the stochastic processes underlying these fluctuations of resonance frequencies. Time correlation functions of (15)N amide chemical shifts computed from molecular dynamics simulations (MD) were analysed in terms of a transiently fractional diffusion process. The analysis of MD trajectories spanning dramatically different time scales (~200 ns and 1ms [Shaw, D. E. et al. Science, 2010, 330, 341-346]) allowed us to show that our model could capture the multiple scale structure of chemical shift fluctuations. Moreover, the predicted exchange contribution Rex to the NMR transverse relaxation rate is in qualitative agreement with experimental results. These observations suggest that the proposed fractional diffusion model may provide significative improvement to the analysis of NMR dispersion experiments.


PMID: 24628040 [PubMed - as supplied by publisher]



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