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.
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 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 ]
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 ...
Proteins are often thought of as relatively stable tertiary structures that experience conformational changes after being affected by interactions with other proteins or as a part of enzymatic activity. However, proteins may have varying degrees of stability, and some of the less stable variants are intrinsically disordered proteins. These ...
The SMC proteins have the potential to form a larger ring-like structure. The ability to create different architectural arrangements allows for various regulations of functions. Some of the possible configurations are double rings, filaments, and rosettes. Double rings are 4 SMC proteins bound at the heads and hinge, forming a ring.