Search results
Results from the WOW.Com Content Network
DNA-binding proteins (2 C, 33 P) E. Enzymes (21 C, 330 P, 1 F) G. ... Pages in category "Proteins by function" The following 9 pages are in this category, out of 9 total.
Especially for enzymes the EC number system provides a functional classification scheme. [31] Similarly, gene ontology classifies both genes and proteins by their biological and biochemical function, and by their intracellular location. [32] Sequence similarity is used to classify proteins both in terms of evolutionary and functional similarity.
The primary structure is held together by peptide bonds that are made during the process of protein biosynthesis. The two ends of the polypeptide chain are referred to as the carboxyl terminus (C-terminus) and the amino terminus (N-terminus) based on the nature of the free group on each
This usually implies that the complex consists of different oligomerisation interfaces. For example, a tetrameric protein may have one four-fold rotation axis, i.e. point group symmetry 4 or C 4. In this case the four interfaces between the subunits are identical. It may also have point group symmetry 222 or D 2. This tetramer has different ...
The number in brackets, called a "sunid", is a SCOP unique integer identifier for each node in the SCOP hierarchy. The number in parentheses indicates how many elements are in each category. For example, there are 284 folds in the "All alpha proteins" class. Each member of the hierarchy is a link to the next level of the hierarchy.
A protein superfamily is the largest grouping of proteins for which common ancestry can be inferred (see homology). Usually this common ancestry is inferred from structural alignment [ 1 ] and mechanistic similarity, even if no sequence similarity is evident. [ 2 ]
In molecular biology, protein fold classes are broad categories of protein tertiary structure topology. They describe groups of proteins that share similar amino acid and secondary structure proportions. Each class contains multiple, independent protein superfamilies (i.e. are not necessarily evolutionarily related to one another). [1] [2] [3]
The common natural forms of amino acids have a zwitterionic structure, with −NH + 3 (−NH + 2 − in the case of proline) and −CO − 2 functional groups attached to the same C atom, and are thus α-amino acids, and are the only ones found in proteins during translation in the ribosome.