Glutamic Acid, Intrinsically Disordered Protein, Protein Function, Protein Structure, Protein-protein Interaction
Digital Object Identifier (DOI)
The ability of a protein to fold into unique functional state or to stay intrinsically disordered is encoded in its amino acid sequence. Both ordered and intrinsically disordered proteins (IDPs) are natural polypeptides that use the same arsenal of 20 proteinogenic amino acid residues as their major building blocks. The exceptional structural plasticity of IDPs, their capability to exist as heterogeneous structural ensembles and their wide array of important disorder-based biological functions that complements functional repertoire of ordered proteins are all rooted within the peculiar differential usage of these building blocks by ordered proteins and IDPs. In fact, some residues (so-called disorder-promoting residues) are noticeably more common in IDPs than in sequences of ordered proteins, which, in their turn, are enriched in several order-promoting residues. Furthermore, residues can be arranged according to their "disorder promoting potencies," which are evaluated based on the relative abundances of various amino acids in ordered and disordered proteins. This review continues a series of publications on the roles of different amino acids in defining the phenomenon of protein intrinsic disorder and concerns glutamic acid, which is the second most disorder-promoting residue.
This work is licensed under a Creative Commons Attribution-Noncommercial 3.0 License
Was this content written or created while at USF?
Citation / Publisher Attribution
Intrinsically Disordered Proteins, v. 1, issue 1, art. e24684
Scholar Commons Citation
Uversky, Vladimir N., "The Alphabet of Intrinsic Disorder: II. Various Roles of Glutamic Acid in Ordered and Intrinsically Disordered Proteins" (2013). Molecular Medicine Faculty Publications. 453.