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Int. J. Mol. Sci. 2009, 10(3), 1360-1368;

Protein Dynamics: From Molecules, to Interactions, to Biology

Center for Biophysics and Computational Biology, Department of Chemistry, Department of Physics, and Beckman Institute for Advanced Science and Technology, 600 South Mathews Ave., Urbana, IL 61801, USA
Received: 19 February 2009 / Revised: 13 March 2009 / Accepted: 17 March 2009 / Published: 20 March 2009
(This article belongs to the Special Issue Protein Folding 2009)
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Proteins have a remarkably rich diversity of dynamical behaviors, and the articles in this issue of the International Journal of Molecular Sciences are a testament to that fact. From the picosecond motions of single sidechains probed by NMR or fluorescence spectroscopy, to aggregation processes at interfaces that take months, all time scales play a role. Proteins are functional molecules, so by their nature they always interact with their environment. This environment includes water, other biomolecules, or larger cellular structures. In a sense, it also includes the protein molecule itself: proteins are large enough to fold and interact with themselves. These interactions have been honed by evolution to produce behaviors completely different from those of random polymers. View Full-Text
Keywords: Downhill folding; evolution; protein function Downhill folding; evolution; protein function
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Gruebele, M. Protein Dynamics: From Molecules, to Interactions, to Biology. Int. J. Mol. Sci. 2009, 10, 1360-1368.

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