The DynaMine webserver: predicting protein dynamics from sequence.

Nucleic Acids Res

Interuniversity Institute of Bioinformatics in Brussels (IB), ULB-VUB, Brussels, Belgium Structural Biology Brussels, Vrije Universiteit Brussel (VUB), Brussels, Belgium Department of Structural Biology, VIB, Brussels, Belgium.

Published: July 2014

AI Article Synopsis

  • Protein dynamics are crucial for understanding how proteins function, but getting accurate data on these movements can be challenging.
  • The DynaMine webserver offers a solution by predicting backbone movements of proteins based on their amino-acid sequences and providing detailed residue-level profiles.
  • This tool allows molecular biologists to compare protein dynamics even without experimental data and makes the prediction results easy to visualize and download.

Article Abstract

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.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4086073PMC
http://dx.doi.org/10.1093/nar/gku270DOI Listing

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