Protein dynamics: from molecules, to interactions, to biology.
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.
Gruebele
Martin
M
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.
D009682:Magnetic Resonance Spectroscopy; D017510:Protein Folding; D060066:Protein Interaction Maps; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D013050:Spectrometry, Fluorescence
D011506:Proteins