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- W897751158 abstract "Intrinsically Disordered Proteins (IDPs) partially or completely lack a co-operatively folded structure under native conditions, preventing their equilibrium state from being adequately described by a single structural model. Our view is that IDPs do possess native structure that is responsible for imparting their specific functions; describing these structures simply requires a broadening of the traditionally narrow structure-function paradigm, beyond the current models developed for cooperatively folding systems. We have shown that 13C direct-detection NMR methods are well suited to generating quantitative and comprehensive structural constraints for IDP ensembles. Generally effective strategies for applying 13C-detected NMR to highly flexible biomolecules will be presented. The structural ensembles we have generated will be discussed in the context of coupled folding and binding interactions, which have arisen as a prevalent mechanism for molecular recognition when IDPs interact with other proteins, or nucleic acids. Many investigators have proposed that a significant loss of chain entropy must oppose the coupled folding and binding process, thus explaining the generally weak (micromolar) binding affinities experimentally measured for IDP-mediated interactions. Synergy between our NMR structural methodology and equilibrium binding measurements will be discussed, suggesting that this view is not generally valid. In contrast, we propose that coupled folding and binding has the characteristics of a bi-molecular protein folding process, driven by a favorable change in solvent entropy." @default.
- W897751158 created "2016-06-24" @default.
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- W897751158 date "2015-04-01" @default.
- W897751158 modified "2023-09-27" @default.
- W897751158 title "Assessing Intrinsically Disordered Protein Structure and Function through Carbon Detected NMR" @default.
- W897751158 doi "https://doi.org/10.1096/fasebj.29.1_supplement.372.2" @default.
- W897751158 hasPublicationYear "2015" @default.
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