Search results
Results from the WOW.Com Content Network
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 ...
Homology model of the DHRS7B protein created with Swiss-model and rendered with PyMOL. Homology modeling, also known as comparative modeling of protein, refers to constructing an atomic-resolution model of the "target" protein from its amino acid sequence and an experimental three-dimensional structure of a related homologous protein (the "template").
Swiss-model pipeline comprises the four main steps that are involved in building a homology model of a given protein structure: Identify structural template(s). BLAST and HHblits are used to identify templates. Those are stored in the Swiss-model Template Library (SMTL), which is derived from Protein Data Bank (PDB). Align target sequence and ...
The fourth is a great example of how interactive graphical tools enable a worker involved in sequence analysis to conveniently execute a variety if different computational tools to explore an alignment's phylogenetic implications; or, to predict the structure and functional properties of a specific sequence, e.g., comparative modelling.
The prediction is made by "threading" (i.e. placing, aligning) each amino acid in the target sequence to a position in the template structure, and evaluating how well the target fits the template. After the best-fit template is selected, the structural model of the sequence is built based on the alignment with the chosen template.
This template is intended for use on protein structure pages. To insert, use {{Protein structure}}. On the primary, secondary, tertiary and quaternary structure pages, it displays alternative versions of the image with the relevant section highlighted. Alternatively, for the non-interactive image, use [[File:Protein structure (full)-en.svg]]
I-TASSER (Iterative Threading ASSEmbly Refinement) is a bioinformatics method for predicting three-dimensional structure model of protein molecules from amino acid sequences. [1] It detects structure templates from the Protein Data Bank by a technique called fold recognition (or threading ).
The structure of a prokaryotic operon of protein-coding genes. Regulatory sequence controls when expression occurs for the multiple protein coding regions (red). Promoter, operator and enhancer regions (yellow) regulate the transcription of the gene into an mRNA. The mRNA untranslated regions (blue) regulate translation into the final protein ...