Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học Critical Care giúp cho các bạn có thêm kiến thức về ngành y học đề tài: Evolutionary potentials: structure specific knowledge-based potentials exploiting the evolutionary record of sequence homologs. | Open Access Method Evolutionary potentials structure specific knowledge-based potentials exploiting the evolutionary record of sequence homologs Alejandro Panjkovich Francisco Melo and Marc A Marti-Renom Addresses Departamento de Genética Molecular y Microbiología Facultad de Ciencias Biológicas Pontificia Universidad Católica de Chile Alameda 340 Santiago Chile. Structural Genomics Unit Bioinformatics Department Centro de Investigación Príncipe Felipe CIPF Av. Autopista del Saler 16 46013 Valencia Spain. Current address Institute for Research in Biomedicine IRB and Barcelona Supercomputing Center BSC c Josep Samitier 1-5 08028 Barcelona Spain. Correspondence Francisco Melo. Email fmelo@. Marc A Marti-Renom. Email mmarti@ Published 8 April 2008 Genome Biology 2008 9 R68 doi 186 gb-2008-9-4-r68 The electronic version of this article is the complete one and can be found online at http 2008 9 4 R68 Received 13 March 2008 Revised 2 April 2008 Accepted 8 April 2008 2008 Panjkovich et al. licensee BioMed Central Ltd. This is an open access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract We introduce a new type of knowledge-based potentials for protein structure prediction called evolutionary potentials which are derived using a single experimental protein structure and all three-dimensional models of its homologous sequences. The new potentials have been benchmarked against other knowledge-based potentials resulting in a significant increase in accuracy for model assessment. In contrast to standard knowledge-based potentials we propose that evolutionary potentials capture key determinants of thermodynamic stability and specific sequence constraints required for fast folding. Background Comparative protein structure prediction is .
