Conformational dynamics of proteins: beyond the nanosecond time scale
Protein motions and functional processes in proteins occur on a wide range of time scales. The fastest atomic motions take place on a femtosecond time scale. Fast biochemical reactions like the primary steps in photosynthesis last few picoseconds. Most biochemical reactions like enzymatic processes take much longer — microseconds or even few milliseconds. They are often accompanied by larger structural rearrangements in the protein, called conformational transitions[l], which are characterized by transition times of nanoseconds or much longer. A prominent example for an extremely slow conformational transition, with a transition time of many years, is the one which is believed to be responsible for the pathogenic effect of prions. Often, conformational transitions constitute functional important motions, as for the gating of channel proteins or in protein folding.
KeywordsAssure Photosynthesis Macromolecule Braunstein Rase
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- H. Grubmüller, P. Tavan, J. Chem. Phys. (Sept. 1994). In press.Google Scholar
- H. Grubmüller, thesis, Technische Universität München (Jan. 1994).Google Scholar
- H. Frauenfelder, Biophys. J. 47 (1985) 35.Google Scholar
- N. Go, T. Noguti, Chem. Scr. 29A (1989) 151.Google Scholar
- N. Ehrenhofer, thesis, Ludwig-Maximilians-Universität München (1994).Google Scholar
- D. R. Dersch, P. Tavan, “Control of annealing in minimal free energy vector quantization”, Proceedings of the IEEE International Conference on Neural Networks ICNN’94, S. K. Orlando, Florida, June 28-July 2, 1994, Rogers and D. W. Ruck, Eds. (IEEE, Piscataway, U.S.A, 1994) pp. 698–703.Google Scholar