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- W2898049514 endingPage "136" @default.
- W2898049514 startingPage "101" @default.
- W2898049514 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." @default.
- W2898049514 created "2018-10-26" @default.
- W2898049514 creator A5012757416 @default.
- W2898049514 creator A5061430976 @default.
- W2898049514 date "2018-01-01" @default.
- W2898049514 modified "2023-10-04" @default.
- W2898049514 title "Using NMR Chemical Shifts to Determine Residue-Specific Secondary Structure Populations for Intrinsically Disordered Proteins" @default.
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