Toward the unification of sequence and structural data for identification of structural and functional constraints.
The identification and characterization of local residue patterns or conserved segments shared by a set of biopolymers has provided a number of insights in molecular biology. Biopolymer sequences are observations from macro molecules that share common structural or function features. The approach taken here rests on the notion that information may be most efficiently extracted from these observations through the use of a model that faithfully represents macro-molecular characteristics. Accordingly, our efforts are focused on statistical models which attempt to capture central features of protein structure, function, and change. Here the assumptions that underlie two new methods for the analysis of protein sequence data are explicitly delineated. (1) Threading of a sequence through structural motifs seeks to determine if a protein sequence fits a known protein structure. The assumptions delineated here also generally apply to other contact based threading methods that have been recently described. (2) Multiple sequence alignment via the Gibbs sampling algorithm seeks to identify position specific empirical free energy models for residue sites in common motifs and simultaneously the align sequence observations form these motifs.
Lawrence
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Wadsworth Labs, NYS-DOH, Albany, NY 12222.
D000465:Algorithms; D000595:Amino Acid Sequence; D000818:Animals; D001699:Biometry; D001704:Biopolymers / Q000737:chemistry; D046911:Macromolecular Substances; D008956:Models, Chemical; D015394:Molecular Structure; D009211:Myoglobin / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D016415:Sequence Alignment / Q000706:statistics & numerical data; D013816:Thermodynamics; D014907:Whales
D001704:Biopolymers; D046911:Macromolecular Substances; D009211:Myoglobin; D011506:Proteins