Author(s): Jamroz M, Kolinski A, Kmiecik S
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Abstract MOTIVATION: Identification of flexible regions of protein structures is important for understanding of their biological functions. Recently, we have developed a fast approach for predicting protein structure fluctuations from a single protein model: the CABS-flex. CABS-flex was shown to be an efficient alternative to conventional all-atom molecular dynamics (MD). In this work, we evaluate CABS-flex and MD predictions by comparison with protein structural variations within NMR ensembles. RESULTS: Based on a benchmark set of 140 proteins, we show that the relative fluctuations of protein residues obtained from CABS-flex are well correlated to those of NMR ensembles. On average, this correlation is stronger than that between MD and NMR ensembles. In conclusion, CABS-flex is useful and complementary to MD in predicting protein regions that undergo conformational changes as well as the extent of such changes. AVAILABILITY AND IMPLEMENTATION: The CABS-flex is freely available to all users at http://biocomp.chem.uw.edu.pl/CABSflex. CONTACT: [email protected]
SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online. © The Author 2014. Published by Oxford University Press.
This article was published in Bioinformatics
and referenced in Journal of Molecular and Genetic Medicine