The DynaMine webserver: predicting protein dynamics from sequence

Protein dynamics are important for understanding protein function. Unfortunately, accurate protein dynamics information is difficult to obtain: here we present the DynaMine webserver, which provides predictions for the fast backbone movements of proteins directly from their amino-acid sequence. Dyna...

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Main Authors: Cilia, Elisa, Pancsa, Rita, Tompa, Peter, Lenaerts, Tom, Vranken, Wim F.
Format: Online
Language:English
Published: Oxford University Press 2014
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4086073/
id pubmed-4086073
recordtype oai_dc
spelling pubmed-40860732014-10-28 The DynaMine webserver: predicting protein dynamics from sequence Cilia, Elisa Pancsa, Rita Tompa, Peter Lenaerts, Tom Vranken, Wim F. Article Protein dynamics are important for understanding protein function. Unfortunately, accurate protein dynamics information is difficult to obtain: here we present the DynaMine webserver, which provides predictions for the fast backbone movements of proteins directly from their amino-acid sequence. DynaMine rapidly produces a profile describing the statistical potential for such movements at residue-level resolution. The predicted values have meaning on an absolute scale and go beyond the traditional binary classification of residues as ordered or disordered, thus allowing for direct dynamics comparisons between protein regions. Through this webserver, we provide molecular biologists with an efficient and easy to use tool for predicting the dynamical characteristics of any protein of interest, even in the absence of experimental observations. The prediction results are visualized and can be directly downloaded. The DynaMine webserver, including instructive examples describing the meaning of the profiles, is available at http://dynamine.ibsquare.be. Oxford University Press 2014-07-01 2014-04-11 /pmc/articles/PMC4086073/ /pubmed/24728994 http://dx.doi.org/10.1093/nar/gku270 Text en © The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/3.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Cilia, Elisa
Pancsa, Rita
Tompa, Peter
Lenaerts, Tom
Vranken, Wim F.
spellingShingle Cilia, Elisa
Pancsa, Rita
Tompa, Peter
Lenaerts, Tom
Vranken, Wim F.
The DynaMine webserver: predicting protein dynamics from sequence
author_facet Cilia, Elisa
Pancsa, Rita
Tompa, Peter
Lenaerts, Tom
Vranken, Wim F.
author_sort Cilia, Elisa
title The DynaMine webserver: predicting protein dynamics from sequence
title_short The DynaMine webserver: predicting protein dynamics from sequence
title_full The DynaMine webserver: predicting protein dynamics from sequence
title_fullStr The DynaMine webserver: predicting protein dynamics from sequence
title_full_unstemmed The DynaMine webserver: predicting protein dynamics from sequence
title_sort dynamine webserver: predicting protein dynamics from sequence
description Protein dynamics are important for understanding protein function. Unfortunately, accurate protein dynamics information is difficult to obtain: here we present the DynaMine webserver, which provides predictions for the fast backbone movements of proteins directly from their amino-acid sequence. DynaMine rapidly produces a profile describing the statistical potential for such movements at residue-level resolution. The predicted values have meaning on an absolute scale and go beyond the traditional binary classification of residues as ordered or disordered, thus allowing for direct dynamics comparisons between protein regions. Through this webserver, we provide molecular biologists with an efficient and easy to use tool for predicting the dynamical characteristics of any protein of interest, even in the absence of experimental observations. The prediction results are visualized and can be directly downloaded. The DynaMine webserver, including instructive examples describing the meaning of the profiles, is available at http://dynamine.ibsquare.be.
publisher Oxford University Press
publishDate 2014
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4086073/
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