Using NMR Chemical Shifts to Determine Residue-specific Secondary Structure Populations for Intrinsically Disordered Proteins
Document Type
Book Chapter
Publication Date
2018
Keywords
Intrinsically Disordered Protein, Intrinsically Disordered Regions, Chemical Shift, Residual Secondary Structure, Transient Secondary Structure, Coupled Folding and Binding, P53 Tumor Suppressor, Myeloblastosis Protein
Digital Object Identifier (DOI)
https://doi.org/10.1016/bs.mie.2018.09.011
Abstract
Protein disorder is a pervasive phenomenon in biology and a natural consequence of polymer evolution that facilitates cell signaling by organizing sites for posttranslational modifications and protein–protein interactions into arrays of short linear motifs that can be rearranged by RNA splicing. Disordered proteins are missing the long-range nonpolar interactions that form tertiary structures, but they often contain regions with residual secondary structure that are stabilized by protein binding. NMR spectroscopy is uniquely suited to detect residual secondary structure in a disordered protein and it can provide atomic resolution data on the structure and dynamics of disordered protein interaction sites. Here we describe how backbone chemical shifts are used for assigning residual secondary structure in disordered proteins and discuss some of the tools available for estimating secondary structure populations with a focus on disordered proteins containing different levels of alpha helical secondary structure which are stabilized by protein binding.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Using NMR Chemical Shifts to Determine Residue-specific Secondary Structure Populations for Intrinsically Disordered Proteins, in E. Rhodes (Ed.), Methods in Enzymology, Academic Press, p. 101-136
Scholar Commons Citation
Borcherds, Wade M. and Daughdrill, Gary W., "Using NMR Chemical Shifts to Determine Residue-specific Secondary Structure Populations for Intrinsically Disordered Proteins" (2018). Molecular Biosciences Faculty Publications. 166.
https://digitalcommons.usf.edu/bcm_facpub/166
