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UniProtKB/Swiss-Prot is a manually annotated, non-redundant protein sequence database. It combines information extracted from scientific literature and biocurator-evaluated computational analysis. The aim of UniProtKB/Swiss-Prot is to provide all known relevant information about a particular protein.
PROSITE is a protein database. [1] [2] It consists of entries describing the protein families, domains and functional sites as well as amino acid patterns and profiles in them.. These are manually curated by a team of the Swiss Institute of Bioinformatics and tightly integrated into Swiss-Prot protein annotati
In 2002, PIR – along with its international partners, the European Bioinformatics Institute and the Swiss Institute of Bioinformatics – were awarded a grant from NIH to create UniProt, a single worldwide database of protein sequence and function, by unifying the Protein Information Resource-Protein Sequence Database, Swiss-Prot, and TrEMBL ...
The UniProt database is an example of a protein sequence database. As of 2013 it contained over 40 million sequences and is growing at an exponential rate. [ 1 ] Historically, sequences were published in paper form, but as the number of sequences grew, this storage method became unsustainable.
The Protein Data Bank was announced in October 1971 in Nature New Biology [10] as a joint venture between Cambridge Crystallographic Data Centre, UK and Brookhaven National Laboratory, US. Upon Hamilton's death in 1973, Tom Koetzle took over direction of the PDB for the subsequent 20 years.
In biology, a protein structure database is a database that is modeled around the various experimentally determined protein structures.The aim of most protein structure databases is to organize and annotate the protein structures, providing the biological community access to the experimental data in a useful way.
Swiss-model (stylized as SWISS-MODEL) is a structural bioinformatics web-server dedicated to homology modeling of 3D protein structures. [ 1 ] [ 2 ] As of 2024 [update] , homology modeling is the most accurate method to generate reliable three-dimensional protein structure models and is routinely used in many practical applications.
Conserved Domain Database is a protein annotation resource that consists of a collection of annotated multiple sequence alignment models for ancient domains and full-length proteins. These are available as position-specific score matrices (PSSMs) for fast identification of conserved domains in protein sequences via RPS-BLAST.