From protein sequence to dynamics and disorder with DynaMine.

TitleFrom protein sequence to dynamics and disorder with DynaMine.
Publication TypeJournal Article
Year of Publication2013
AuthorsCilia, E., Pancsa R., Tompa P., Lenaerts T., and Vranken W. F.
JournalNat Commun
Volume4
Pagination2741
Date Published2013
Type of Articleidp
ISSN2041-1723
KeywordsAlgorithms, Amino Acid Sequence, Humans, Molecular Sequence Data, Protein Conformation, Protein Folding, Proteins, Sequence Alignment, Software
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.

DOI10.1038/ncomms3741
Alternate JournalNat Commun
PubMed ID24225580
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