Int. J. Mol. Sci. 2009, 10(3), 1360-1368; doi:10.3390/ijms10031360
Editorial

Protein Dynamics: From Molecules, to Interactions, to Biology

email
Received: 19 February 2009; in revised form: 13 March 2009 / Accepted: 17 March 2009 / Published: 20 March 2009
(This article belongs to the Special Issue Protein Folding)
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Abstract: 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.
Keywords: Downhill folding; evolution; protein function
PDF Full-text Download PDF Full-Text [164 KB, uploaded 19 June 2014 02:18 CEST]

Export to BibTeX |
EndNote


MDPI and ACS Style

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

AMA Style

Gruebele M. Protein Dynamics: From Molecules, to Interactions, to Biology. International Journal of Molecular Sciences. 2009; 10(3):1360-1368.

Chicago/Turabian Style

Gruebele, Martin. 2009. "Protein Dynamics: From Molecules, to Interactions, to Biology." Int. J. Mol. Sci. 10, no. 3: 1360-1368.

Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert