Cargando…
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...
Autor principal: | |
---|---|
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 |
_version_ | 1782166461203087360 |
---|---|
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. |
format | Text |
id | pubmed-2672034 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | Molecular Diversity Preservation International (MDPI) |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT gruebelemartin proteindynamicsfrommoleculestointeractionstobiology |