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Consistent View of Polypeptide Chain Expansion in Chemical Denaturants from Multiple Experimental Methods.
There has been a long-standing controversy regarding the effect of chemical denaturants on the dimensions of unfolded and intrinsically disordered proteins: A wide range of experimental techniquesExpand
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Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopy
The dimensions of unfolded and intrinsically disordered proteins are highly dependent on their amino acid composition and solution conditions, especially salt and denaturant concentration. However,Expand
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Single-molecule spectroscopy reveals polymer effects of disordered proteins in crowded environments
Significance In the interior of a cell, the volume accessible to each protein molecule is restricted by the presence of the large number of other macromolecules. Such a crowded environment is knownExpand
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Quantifying internal friction in unfolded and intrinsically disordered proteins with single-molecule spectroscopy
Internal friction, which reflects the “roughness” of the energy landscape, plays an important role for proteins by modulating the dynamics of their folding and other conformational changes. However,Expand
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Ultrafast dynamics of protein collapse from single-molecule photon statistics
We use the statistics of photon emission from single molecules to probe the ultrafast dynamics of an unfolded protein via Förster resonance energy transfer. Global reconfiguration of the chain occursExpand
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Extreme disorder in an ultrahigh-affinity protein complex
Molecular communication in biology is mediated by protein interactions. According to the current paradigm, the specificity and affinity required for these interactions are encoded in the preciseExpand
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Single-molecule fluorescence reveals sequence-specific misfolding in multidomain proteins
A large range of debilitating medical conditions is linked to protein misfolding, which may compete with productive folding particularly in proteins containing multiple domains. Seventy-five per centExpand
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Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein
Significance Molecular chaperones are a group of proteins that are essential for avoiding the aggregation of other proteins in the crowded cellular environment. Chaperones function by interactingExpand
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Charge interactions can dominate the dimensions of intrinsically disordered proteins
Many eukaryotic proteins are disordered under physiological conditions, and fold into ordered structures only on binding to their cellular targets. Such intrinsically disordered proteins (IDPs) oftenExpand
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Charge interactions can dominate the dimensions of intrinsically disordered proteins
Many eukaryotic proteins are disordered under physiological conditions, and fold into ordered structures only on binding to their cellular targets. Such intrinsically disordered proteins (IDPs) oftenExpand
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