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The Structural Classification of Proteins database [35] and CATH database [36] provide two different structural classifications of proteins. When the structural similarity is large the two proteins have possibly diverged from a common ancestor, [ 37 ] and shared structure between proteins is considered evidence of homology .
Structural Classification of Proteins database (SCOP) [4] Both classification schemes are based on a hierarchy of fold types. 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.
The classification levels organise more than 41 000 non-redundant domains that represent more than 504 000 protein structures. The Evolutionary Classification of Protein Domains (ECOD) database released in 2014 is a similar to SCOPe expansion of SCOP version 1.75.
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 ...
Protein subfamily is a level of protein classification, based on their close evolutionary relationship. It is below the larger levels of protein superfamily and protein family. [1] Proteins typically share greater sequence and function similarities with other subfamily members than they do with members of their wider family.
Protein quaternary structure [a] is the fourth (and highest) classification level of protein structure.Protein quaternary structure refers to the structure of proteins which are themselves composed of two or more smaller protein chains (also referred to as subunits).
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.