The Intrinsic Disorder Alphabet. III. Dual Personality of Serine
amidase, carboxylesterase, intrinsically disordered protein, protein folding, protein structure, posttranslational modification, serine hydrolase, serine protease
Digital Object Identifier (DOI)
Proteins are natural polypeptides consisting of 20 major amino acid residues, content and order of which in a given amino acid sequence defines the ability of a related protein to fold into unique functional state or to stay intrinsically disordered. Amino acid sequences code for both foldable (ordered) proteins/domains and for intrinsically disordered proteins (IDPs) and IDP regions (IDPRs), but these sequence codes are dramatically different. This difference starts with a very general property of the corresponding amino acid sequences, namely, their compositions. IDPs/IDPRs are enriched in specific disorder-promoting residues, whereas amino acid sequences of ordered proteins/domains typically contain more order-promoting residues. Therefore, the relative abundances of various amino acids in ordered and disordered proteins can be used to scale amino acids according to their disorder promoting potentials. This review continues a series of publications on the roles of different amino acids in defining the phenomenon of protein intrinsic disorder and represents serine, which is the third most disorder-promoting residue. Similar to previous publications, this review represents some physico-chemical properties of serine and the roles of this residue in structures and functions of ordered proteins, describes major posttranslational modifications tailored to serine, and finally gives an overview of roles of serine in structure and functions of intrinsically disordered proteins.
Was this content written or created while at USF?
Citation / Publisher Attribution
Intrinsically Disordered Proteins, v. 3, issue 1, art. e1027032
Scholar Commons Citation
Uversky, Vladimir N., "The Intrinsic Disorder Alphabet. III. Dual Personality of Serine" (2015). Molecular Medicine Faculty Publications. 371.