Ab initio construction of protein tertiary structures using a hierarchical approach. Export

@article{citeulike:1079596, abstract = {We present a hierarchical method to predict protein tertiary structure models from sequence. We start with complete enumeration of conformations using a simple tetrahedral lattice model. We then build conformations with increasing detail, and at each step select a subset of conformations using empirical energy functions with increasing complexity. After enumeration on lattice, we select a subset of low energy conformations using a statistical residue-residue contact energy function, and generate all-atom models using predicted secondary structure. A combined knowledge-based atomic level energy function is then used to select subsets of the all-atom models. The final predictions are generated using a consensus distance geometry procedure. We test the feasibility of the procedure on a set of 12 small proteins covering a wide range of protein topologies. A rigorous double-blind test of our method was made under the auspices of the CASP3 experiment, where we did ab initio structure predictions for 12 proteins using this approach. The performance of our methodology at CASP3 is reasonably good and completely consistent with our initial tests.}, address = {Department of Structural Biology, Stanford University School of Medicine, Stanford, CA, 94305, USA.}, author = {Xia, Y. and Huang, E. S. and Levitt, M. and Samudrala, R.}, citeulike-article-id = {1079596}, citeulike-linkout-0 = {http://dx.doi.org/10.1006/jmbi.2000.3835}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/10864507}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=10864507}, citeulike-linkout-3 = {http://www.sciencedirect.com/science/article/B6WK7-45F51FD-DR/2/8971f0378710a912aa28c75071b1fd7b}, day = {30}, doi = {10.1006/jmbi.2000.3835}, issn = {0022-2836}, journal = {J Mol Biol}, keywords = {folding, protein}, month = {June}, number = {1}, pages = {171--185}, posted-at = {2008-01-11 02:45:22}, priority = {2}, title = {Ab initio construction of protein tertiary structures using a hierarchical approach.}, url = {http://dx.doi.org/10.1006/jmbi.2000.3835}, volume = {300}, year = {2000} }

TY - JOUR ID - citeulike:1079596 L3 - citeulike-article-id:1079596 N2 - We present a hierarchical method to predict protein tertiary structure models from sequence. We start with complete enumeration of conformations using a simple tetrahedral lattice model. We then build conformations with increasing detail, and at each step select a subset of conformations using empirical energy functions with increasing complexity. After enumeration on lattice, we select a subset of low energy conformations using a statistical residue-residue contact energy function, and generate all-atom models using predicted secondary structure. A combined knowledge-based atomic level energy function is then used to select subsets of the all-atom models. The final predictions are generated using a consensus distance geometry procedure. We test the feasibility of the procedure on a set of 12 small proteins covering a wide range of protein topologies. A rigorous double-blind test of our method was made under the auspices of the CASP3 experiment, where we did ab initio structure predictions for 12 proteins using this approach. The performance of our methodology at CASP3 is reasonably good and completely consistent with our initial tests. IS - 1 JF - J Mol Biol SN - 0022-2836 AD - Department of Structural Biology, Stanford University School of Medicine, Stanford, CA, 94305, USA. EP - 185 TI - Ab initio construction of protein tertiary structures using a hierarchical approach. VL - 300 SP - 171 KW - folding KW - protein AU - Xia, Y AU - Huang, ES AU - Levitt, M AU - Samudrala, R PY - 2000/06/30/ UR - http://dx.doi.org/10.1006/jmbi.2000.3835 ER -