Disorder for Dummies: Functional Mutagenesis of Transient Helical Segments in Disordered Proteins
Document Type
Book Chapter
Publication Date
2020
Keywords
Protein Disorder, Transient Helicity, α-helix, Protein Evolution, Protein–protein Interactions, IDP CD Spectroscopy, NMR
Digital Object Identifier (DOI)
https://doi.org/10.1007/978-1-0716-0524-0_1
Abstract
Most cytosolic eukaryotic proteins contain a mixture of ordered and disordered regions. Disordered regions facilitate cell signaling by concentrating sites for posttranslational modifications and protein–protein interactions into arrays of short linear motifs that can be reorganized by RNA splicing. The evolution of disordered regions looks different from their ordered counterparts. In some cases, selection is focused on maintaining protein binding interfaces and PTM sites, but sequence heterogeneity is common. In other cases, simple properties like charge, length, or end-to-end distance are maintained. Many disordered protein binding sites contain some transient secondary structure that may resemble the structure of the bound state. α-Helical secondary structure is common and a wide range of fractional helicity is observed in different disordered regions. Here we provide a simple protocol to identify transient helical segments and design mutants that can change their structure and function.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Disorder for Dummies: Functional Mutagenesis of Transient Helical Segments in Disordered Proteins, in B. B. Kragelund & K. Skriver (Eds.), Intrinsically Disordered Proteins, Humana, p. 3-20
Scholar Commons Citation
Daughdrill, Gary W., "Disorder for Dummies: Functional Mutagenesis of Transient Helical Segments in Disordered Proteins" (2020). Molecular Biosciences Faculty Publications. 170.
https://digitalcommons.usf.edu/bcm_facpub/170
