High accuracy protein modeling from its sequence information is an important step toward revealing the sequence-structure-function relationship of proteins and nowadays it becomes increasingly more useful for practical purposes such as in drug discovery and in protein design. We have developed a protocol for protein structure prediction that can generate highly accurate protein models in terms of backbone structure, side-chain orientation, hydrogen bonding, and binding sites of ligands. To obtain accurate protein models, we have combined a powerful global optimization method with traditional homology modeling procedures such as multiple sequence alignment, chain building, and side-chain remodeling. We have built a series of specific score functions for these steps, and optimized them by utilizing conformational space annealing, which is one of the most successful combinatorial optimization algorithms currently available. © 2011 Springer Science+Business Media,LLC.
CITATION STYLE
Joo, K., Lee, J., & Lee, J. (2012). Methods for accurate homology modeling by global optimization. Methods in Molecular Biology, 857, 175–188. https://doi.org/10.1007/978-1-61779-588-6_7
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