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NMR Relaxation in Proteins with Fast Internal Motions and Slow Conformational Exchange: Model-Free Framework and Markov State Simulations
2013
Journal of Physical Chemistry B
Calculating NMR relaxation effects for proteins with dynamics on multiple timescales generally requires very long trajectories based on conventional molecular dynamics simulations. In this report, we have built Markov state models from multiple MD trajectories and used the resulting MSM to capture the very fast internal motions of the protein within a free energy basin on a time scale up to hundreds of picoseconds and the more than three orders of magnitude slower conformational exchange
doi:10.1021/jp400797y
pmid:23638941
pmcid:PMC3727231
fatcat:gtdo4vxbp5gpxh4kqzka6fiig4