Abstract
Intrinsically disordered proteins (IDPs) are enriched in polar and charged amino acids and lack a single, well-defined tertiary structure. IDPs are frequently the targets of post-translational modifications (PTMs) which can affect protein folding or stability, activity, susceptibility to degradation, and function. Phosphorylation is one of the most common PTMs and occurs on serine, threonine, and tyrosine residues. Hyperphosphorylation of some IDPs is associated with disease states, such as the tau protein in Alzheimer’s disease and α-synuclein in Parkinson’s disease.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
