Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 99, Issue 11, Pages 7432-7437Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.102179699
Keywords
force field; energy minimization; protein structure prediction
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Funding
- NIGMS NIH HHS [GM-30518, R37 GM030518, R01 GM030518] Funding Source: Medline
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In this paper, we introduce a method to account for the shape of the potential energy curve in the evaluation of conformational free energies. The method is based on a procedure that generates a set of conformations, each with its own force-field energy, but adds a term to this energy that favors conformations that are close in structure (have a low rmsd) to other conformations. The sum of the force-field energy and rmsd-dependent term is defined here as the colony energy of a given conformation, because each conformation that is generated is viewed as representing a colony of points. The use of the colony energy tends to select conformations that are located in broad energy basins. The approach is applied to the ab initio prediction of the conformations of all of the loops in a dataset of 135 nonredundant proteins. By using an rmsd from a native criterion based on the superposition of loop stems, the average rmsd of 5-, 6-, 7-, and 8-residue long loops is 0.85, 0.92, 1.23, and 1.45 Angstrom, respectively. For 8-residue loops, 60 of 61 predictions have an rmsd of less than 3.0 Angstrom. The use of the colony energy is found to improve significantly the results obtained from the potential function alone. (The loop prediction program, Loopy, can be downloaded at http://trantor.bioc.columbia.edu.)
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