Nano Futures · 2021 · 11 citations · 67 references
Life SciencesBiochemistryBiophysicsProtein FoldingProteomicsStructural BiologyIntrinsic DisorderIntrinsically Disordered ProteinsProtein DenaturationProtein DynamicsProtein Folding DynamicsProtein StructureDenatured State EnsembleDisordered ProteinsIntrinsic Disorder To Structure TransitionIntrinsically Disordered DomainsProtein Disorder Dynamics
Abstract The human proteome is enriched in proteins that do not fold into a stable 3D structure. These intrinsically disordered proteins (IDPs) spontaneously fluctuate between a large number of configurations in their native form. Remarkably, the disorder does not lead to dysfunction as with denatured folded proteins. In fact, unlike denatured proteins, recent evidence strongly suggests that multiple biological functions stem from such structural plasticity. Here, focusing on the nanometer length-scale, we review the latest advances in IDP research and discuss some of the future directions in this highly promising field.
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Fluorescence correlation spectroscopy. I. Conceptual basis and theory
Elliot L. Elson, Douglas Magde · Biopolymers · 1974 · 1.4K citations
Natural Sciences, Chemistry, Physics +17