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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 i...

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Detalles Bibliográficos
Autor principal: Gruebele, Martin
Formato: Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2672034/
https://www.ncbi.nlm.nih.gov/pubmed/19399253
http://dx.doi.org/10.3390/ijms10031360
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author Gruebele, Martin
author_facet Gruebele, Martin
author_sort Gruebele, Martin
collection PubMed
description 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.
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spelling pubmed-26720342009-04-27 Protein Dynamics: From Molecules, to Interactions, to Biology Gruebele, Martin Int J Mol Sci Editorial 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. Molecular Diversity Preservation International (MDPI) 2009-03-20 /pmc/articles/PMC2672034/ /pubmed/19399253 http://dx.doi.org/10.3390/ijms10031360 Text en © 2009 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Editorial
Gruebele, Martin
Protein Dynamics: From Molecules, to Interactions, to Biology
title Protein Dynamics: From Molecules, to Interactions, to Biology
title_full Protein Dynamics: From Molecules, to Interactions, to Biology
title_fullStr Protein Dynamics: From Molecules, to Interactions, to Biology
title_full_unstemmed Protein Dynamics: From Molecules, to Interactions, to Biology
title_short Protein Dynamics: From Molecules, to Interactions, to Biology
title_sort protein dynamics: from molecules, to interactions, to biology
topic Editorial
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2672034/
https://www.ncbi.nlm.nih.gov/pubmed/19399253
http://dx.doi.org/10.3390/ijms10031360
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