From protein sequence to dynamics and disorder with DynaMine

Elisa Cilia, Rita Pancsa, Peter Tompa, Tom Lenaerts and Wim F. Vranken ()
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Elisa Cilia: MLG, Université Libre de Bruxelles
Rita Pancsa: Structural Biology Brussels, Vrije Universiteit Brussel
Peter Tompa: Interuniversity Institute of Bioinformatics in Brussels, ULB-VUB, La Plaine Campus
Tom Lenaerts: MLG, Université Libre de Bruxelles
Wim F. Vranken: Interuniversity Institute of Bioinformatics in Brussels, ULB-VUB, La Plaine Campus

Nature Communications, 2013, vol. 4, issue 1, 1-10

Abstract: Abstract Protein function and dynamics are closely related; however, accurate dynamics information is difficult to obtain. Here based on a carefully assembled data set derived from experimental data for proteins in solution, we quantify backbone dynamics properties on the amino-acid level and develop DynaMine—a fast, high-quality predictor of protein backbone dynamics. DynaMine uses only protein sequence information as input and shows great potential in distinguishing regions of different structural organization, such as folded domains, disordered linkers, molten globules and pre-structured binding motifs of different sizes. It also identifies disordered regions within proteins with an accuracy comparable to the most sophisticated existing predictors, without depending on prior disorder knowledge or three-dimensional structural information. DynaMine provides molecular biologists with an important new method that grasps the dynamical characteristics of any protein of interest, as we show here for human p53 and E1A from human adenovirus 5.

Date: 2013
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DOI: 10.1038/ncomms3741

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