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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 annotation.
The PROSITE notation uses the IUPAC one-letter codes and conforms to the above description with the exception that a concatenation symbol, '-', is used between pattern elements, but it is often dropped between letters of the pattern alphabet. PROSITE allows the following pattern elements in addition to those described previously:
Adobe Portfolio (formerly ProSite) is Behance's DIY web design application, similar to popular tools such as Weebly and Joomla. It is a personal portfolio site creation tool on the web and it syncs with a user's Behance project. [14] Adobe Portfolio can only be accessed by buying an Adobe Creative Cloud subscription.
InterPro is a database of protein families, protein domains and functional sites in which identifiable features found in known proteins can be applied to new protein sequences [2] in order to functionally characterise them.
The [Fe 4 S 4] clusters are abundant cofactors of metalloproteins. [5] They participate in electron-transfer sequences. The core structure for the [Fe 4 S 4] cluster is a cube with alternating Fe and S vertices.
This is template for a protein family/domain as defined in biological databases such as Pfam. Template parameters [Edit template data] Parameter Description Type Status Symbol Symbol no description Line optional Name Name no description Line optional Image image fill in "NONE" if not needed to suppress the tracking category File optional Width width Width for image String optional Caption ...
Molecular chaperones are a diverse family of proteins that function to protect proteins from irreversible aggregation during synthesis and in times of cellular stress.The bacterial molecular chaperone DnaK is an enzyme that couples cycles of ATP binding, hydrolysis, and ADP release by an N-terminal ATP-hydrolyzing domain to cycles of sequestration and release of unfolded proteins by a C ...
In molecular biology the LysM domain is a protein domain found in a wide variety of extracellular proteins and receptors. The LysM domain is named after the Lysin Motif which was the original name given to the sequence motif identified in bacterial proteins.