Population shuffling of protein conformations.
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.
Dept. for NMR-based Structural Biology, Max-Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen (Germany); Dept. for Theoretical and Computational Biophysics, Max-Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen (Germany).
Colin A
CA
Smith
David
D
Ban
Supriya
S
Pratihar
Karin
K
Giller
Claudia
C
Schwiegk
Bert L
BL
de Groot
Stefan
S
Becker
Christian
C
Griesinger
Donghan
D
Lee
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D006801:Humans; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D009038:Motion; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D013291:Streptococcus / Q000737:chemistry*; D013816:Thermodynamics; D025801:Ubiquitin / Q000737:chemistry*
D001426:Bacterial Proteins; C034284:IgG Fc-binding protein, Streptococcus; D025801:Ubiquitin
conformation; kinetics; protein dynamics; relaxation dispersion; thermodynamics