A Score of the Ability of a Three-Dimensional Protein Model to Retrieve Its Own Sequence as a Quantitative Measure of Its Quality and Appropriateness
Por:
Martinez-Castilla, LP, Rodriguez-Sotres, R
Publicada:
7 sep 2010
Resumen:
Background: Despite the remarkable progress of bioinformatics, how the primary structure of a protein leads to a three-dimensional fold, and in turn determines its function remains an elusive question. Alignments of sequences with known function can be used to identify proteins with the same or similar function with high success. However, identification of function-related and structure-related amino acid positions is only possible after a detailed study of every protein. Folding pattern diversity seems to be much narrower than sequence diversity, and the amino acid sequences of natural proteins have evolved under a selective pressure comprising structural and functional requirements acting in parallel. Principal Findings: The approach described in this work begins by generating a large number of amino acid sequences using ROSETTA [Dantas G et al. (2003) J Mol Biol 332: 449-460], a program with notable robustness in the assignment of amino acids to a known three-dimensional structure.
Filiaciones:
Martinez-Castilla, LP:
Univ Nacl Autonoma Mexico, Fac Quim, Dept Bioquim, Mexico City 04510, DF, Mexico
Univ Nacl Autonoma Mexico, Ctr Ciencias Complejidad, Mexico City 04510, DF, Mexico
Rodriguez-Sotres, R:
Univ Nacl Autonoma Mexico, Fac Quim, Dept Bioquim, Mexico City 04510, DF, Mexico
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