Search results
Results from the WOW.Com Content Network
At the top level are all alpha proteins (domains consisting of alpha helices), all beta proteins (domains consisting of beta sheets), and mixed alpha helix/beta sheet proteins. While most proteins adopt a single stable fold, a few proteins can rapidly interconvert between one or more folds. These are referred to as metamorphic proteins. [5]
The Structural Classification of Proteins (SCOP) database is a largely manual classification of protein structural domains based on similarities of their structures and amino acid sequences. A motivation for this classification is to determine the evolutionary relationship between proteins.
α/β proteins are a class of structural domains in which the secondary structure is composed of alternating α-helices and β-strands along the backbone. The β-strands are therefore mostly parallel. [4] Common examples include the flavodoxin fold, the TIM barrel and leucine-rich-repeat (LRR) proteins such as ribonuclease inhibitor.
The study of proteins, generally under the heading of proteomics, is a vast and complex subject, and much effort has been made to classify and categorize, according to the many specific fields of investigation under which they come.
The CATH Protein Structure Classification database is a free, publicly available online resource that provides information on the evolutionary relationships of protein domains. It was created in the mid-1990s by Professor Christine Orengo and colleagues including Janet Thornton and David Jones , [ 2 ] and continues to be developed by the Orengo ...
Protein domains allow protein classification by a combination of sequence, structure and function, and they can be combined in many ways. In an early study of 170,000 proteins, about two-thirds were assigned at least one domain, with larger proteins containing more domains (e.g. proteins larger than 600 amino acids having an average of more ...
Some protein dynamics [8] and conformational changes of the protein structure may also be conserved, as is seen in the serpin superfamily. [9] Consequently, protein tertiary structure can be used to detect homology between proteins even when no evidence of relatedness remains in their sequences.
A successful search yields the class, folds, superfamilies, families, and individual proteins matching the query. Domain Assignments The database has domain assignments, alignments, and architectures for completely sequence eukaryotic and prokaryotic organisms, plus sequence collections.