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- W2914187897 abstract "Adaptive mutations that alter the functionality of proteins are enriched within intrinsically disordered protein regions (IDRs), thus conformational flexibility appears to translate to evolvability. Pre-structured motifs (PreSMos) with relatively low propensity for secondary structure conformation are believed to be important for IDR function, particularly coupled binding and folding protein interactions. A set of 60 change-of-function mutants affecting the intrinsically disordered 58-residue glucocorticoid receptor tau1core transcriptional activation domain (GRtau1core) were studied using disorder prediction algorithms, NMR spectroscopy and molecular dynamics simulations. Overall we conclude that changes in PreSMo stability account for the effects of a subset of change-of-function mutants affecting the GRtau1core IDR." @default.
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- W2914187897 date "2019-02-01" @default.
- W2914187897 modified "2023-09-30" @default.
- W2914187897 title "Functional Adaptation Mutations Alter Propensity for Alpha-Helical Conformation in the Intrinsically Disordered Glucocorticoid Receptor Tau1Core Activation Domain" @default.
- W2914187897 doi "https://doi.org/10.1016/j.bpj.2018.11.996" @default.
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