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Population Shuffling of Protein Conformations
Authors:Dr Colin A Smith  Dr David Ban  Supriya Pratihar  Karin Giller  Claudia Schwiegk  Prof Dr Bert L de Groot  Dr Stefan Becker  ProfDr Christian Griesinger  Dr Donghan Lee
Institution:1. Dept. for NMR‐based Structural Biology, Max‐Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 G?ttingen (Germany);2. Dept. for Theoretical and Computational Biophysics, Max‐Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 G?ttingen (Germany);3. Present Address: Dept. for Structural Biology, St. Jude Children's Research Hospital, 262 Danny Thomas Place, Memphis, TN 38105 (USA)
Abstract:Motions play a vital role in the functions of many proteins. Discrete conformational transitions to excited states, happening on timescales of hundreds of microseconds, have been extensively characterized. On the other hand, the dynamics of the ground state are widely unexplored. Newly developed high‐power relaxation dispersion experiments allow the detection of motions up to a one‐digit microsecond timescale. These experiments showed that side chains in the hydrophobic core as well as at protein–protein interaction surfaces of both ubiquitin and the third immunoglobulin binding domain of protein G move on the microsecond timescale. Both proteins exhibit plasticity to this microsecond motion through redistribution of the populations of their side‐chain rotamers, which interconvert on the picosecond to nanosecond timescale, making it likely that this “population shuffling” process is a general mechanism.
Keywords:conformation  kinetics  protein dynamics  relaxation dispersion  thermodynamics
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