Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 109, Issue 26, Pages 10340-10345Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1207864109
Keywords
protein folding; residue contact prediction; contact map estimation; residue-residue coevolution; statistical potentials
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Funding
- National Science Foundation through the Center for Theoretical Biological Physics [PHY-0822283, NSF-MCB-1214457]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1214457] Funding Source: National Science Foundation
- Division Of Physics
- Direct For Mathematical & Physical Scien [1308264] Funding Source: National Science Foundation
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We introduce a theoretical framework that exploits the ever-increasing genomic sequence information for protein structure prediction. Structure-based models are modified to incorporate constraints by a large number of non-local contacts estimated from direct coupling analysis (DCA) of co-evolving genomic sequences. A simple hybrid method, called DCA-fold, integrating DCA contacts with an accurate knowledge of local information (e. g., the local secondary structure) is sufficient to fold proteins in the range of 1-3 angstrom resolution.
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