Sequence patterns derived from the automated prediction of functional residues in structurally-aligned homologous protein families
Author(s) -
Ricardo Núñez Miguel
Publication year - 2004
Publication title -
bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.599
H-Index - 390
eISSN - 1367-4811
pISSN - 1367-4803
DOI - 10.1093/bioinformatics/bth255
Subject(s) - protein superfamily , sequence (biology) , function (biology) , computational biology , sequence alignment , structural classification of proteins database , sequence database , biology , conserved sequence , protein family , protein sequencing , sequence analysis , peptide sequence , protein structure , computer science , genetics , biochemistry , gene
Most proteins have evolved to perform specific functions that are dependent on the adoption of well-defined three-dimensional (3D) structures. Specific patterns of conserved residues in amino acid sequences of divergently evolved proteins are frequently observed; these may reflect evolutionary restraints arising both from the need to maintain tertiary structure and the requirement to conserve residues more directly involved in function. Databases of such sequence patterns are valuable in identifying distant homologues, in predicting function and in the study of evolution.
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