Title |
Scoring docking conformations using predicted protein interfaces
|
---|---|
Published in |
BMC Bioinformatics, June 2014
|
DOI | 10.1186/1471-2105-15-171 |
Pubmed ID | |
Authors |
Reyhaneh Esmaielbeiki, Jean-Christophe Nebel |
Abstract |
Since proteins function by interacting with other molecules, analysis of protein-protein interactions is essential for comprehending biological processes. Whereas understanding of atomic interactions within a complex is especially useful for drug design, limitations of experimental techniques have restricted their practical use. Despite progress in docking predictions, there is still room for improvement. In this study, we contribute to this topic by proposing T-PioDock, a framework for detection of a native-like docked complex 3D structure. T-PioDock supports the identification of near-native conformations from 3D models that docking software produced by scoring those models using binding interfaces predicted by the interface predictor, Template based Protein Interface Prediction (T-PIP). |
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Geographical breakdown
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Norway | 1 | 50% |
Unknown | 1 | 50% |
Demographic breakdown
Type | Count | As % |
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Scientists | 1 | 50% |
Members of the public | 1 | 50% |
Mendeley readers
Geographical breakdown
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United Kingdom | 3 | 5% |
Switzerland | 1 | 2% |
Denmark | 1 | 2% |
Spain | 1 | 2% |
United States | 1 | 2% |
Unknown | 49 | 88% |
Demographic breakdown
Readers by professional status | Count | As % |
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Student > Ph. D. Student | 21 | 38% |
Student > Master | 10 | 18% |
Researcher | 8 | 14% |
Student > Postgraduate | 4 | 7% |
Professor > Associate Professor | 4 | 7% |
Other | 6 | 11% |
Unknown | 3 | 5% |
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Biochemistry, Genetics and Molecular Biology | 11 | 20% |
Computer Science | 7 | 13% |
Chemistry | 4 | 7% |
Pharmacology, Toxicology and Pharmaceutical Science | 2 | 4% |
Other | 9 | 16% |
Unknown | 4 | 7% |