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.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Cilia E,Pancsa R,Tompa P,Lenaerts T,Vranken WFdoi
10.1038/ncomms3741subject
Has Abstractpub_date
2013-01-01 00:00:00pages
2741issn
2041-1723pii
ncomms3741journal_volume
4pub_type
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