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To predict the function, structure, or other properties of a protein for which only its sequence of amino acids is known, the protein sequence is compared to the sequences of other proteins in public databases. If a protein with sufficiently similar sequence is found, the two proteins are likely to be evolutionarily related ("homologous"). In ...
With BAR 3.0 and a sequence you can annotate when possible: function (Gene Ontology), structure (Protein Data Bank), protein domains (Pfam). Also if your sequence falls into a cluster with a structural/some structural template/s we provide an alignment towards the template/templates based on the Cluster-HMM (HMM profile) that allows you to ...
Rosetta homology modeling and ab initio fragment assembly with Ginzu domain prediction: Webserver Rosetta@home: Distributed-computing implementation of Rosetta algorithm: Downloadable program Abalone: Molecular Dynamics folding: Program C-QUARK C-QUARK is a method for ab initio protein structure prediction. Based on deep-learning based contact ...
A step called domain parsing, or domain boundary prediction, is usually done first to split a protein into potential structural domains. As with the rest of tertiary structure prediction, this can be done comparatively from known structures [ 32 ] or ab initio with the sequence only (usually by machine learning , assisted by covariation). [ 33 ]
Describes protein families and domain architectures in complete genomes. Protein families are formed using a Markov clustering algorithm, followed by multi-linkage clustering according to sequence identity. Mapping of predicted structure and sequence domains is undertaken using hidden Markov models libraries representing CATH and Pfam domains ...
Sequence alignment by genetic algorithm: Protein: Local or global: C. Notredame et al. 1996 (new version 1998) SAM Hidden Markov model: Protein: Local or global: A. Krogh et al. 1994 (most recent version 2002) Se-Al Manual alignment: Both: Local: A. Rambaut: 2002: StatAlign Bayesian co-estimation of alignment and phylogeny (MCMC) Both: Global ...
Structure based prediction of fribrillation propoensities, using crystal strucutrue of the fibril forming peptide NNQQNY from the sup 35 prion protein of Saccharomyces cerevisiae. sequence - Amyloidogenic regions and, energy and beta-sheet conformation STITCHER [24] 2012 Web Server - Stitcher (currently offline) Secondary structure-related ...
A profile HMM modelling a multiple sequence alignment. HMMER is a free and commonly used software package for sequence analysis written by Sean Eddy. [2] Its general usage is to identify homologous protein or nucleotide sequences, and to perform sequence alignments.