AI Article Synopsis
- Protein dynamics are crucial for understanding protein function, but collecting accurate data has been challenging.
- The authors introduce DynaMine, a new tool that predicts protein backbone dynamics using only the protein's sequence, enabling the identification of various structural regions and disordered areas.
- DynaMine's predictions are highly accurate, offering molecular biologists a valuable resource for studying the dynamics of proteins, exemplified by applications to the human p53 and E1A proteins.
Article 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.
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| http://dx.doi.org/10.1038/ncomms3741 | DOI Listing |
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