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- W2236673934 abstract "Russell C. Goodman and Theresa L. Beaty Department of Chemistry and Physics, Le Moyne College, 1419 Salt Springs Road, Syracuse, NY 13214 Introduction Intrinsically disordered proteins (IDPs) are a novel class of proteins that, until over a decade ago, had not been recognized as a functional class of proteins. As opposed to globular and lipidsoluble proteins, IDPs lack a well defined structure. In solution, an IDP adopts an ensemble of conformations; however, when bound to a ligand, an IDP adopts a particular structure with a particular function. Disordered proteins my bind a multitude of ligands, exhibiting what is referred to as binding promiscuity (Uversky 2005). Therefore, rather than adhering strictly to the classical structure-function paradigm associated with globular proteins, IDPs can adopt multiple structures, each possessing a different function." @default.
- W2236673934 created "2016-06-24" @default.
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- W2236673934 date "2011-03-24" @default.
- W2236673934 modified "2023-09-26" @default.
- W2236673934 title "Prediction of binding sites on intrinsically disordered proteins" @default.
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- W2236673934 doi "https://doi.org/10.7490/f1000research.906.1" @default.
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