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Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy
Protein folding is inherently a heterogeneous process because of the very large number of microscopic pathways that connect the myriad unfolded conformations to the unique conformation of the nativeExpand
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Neural activity associated with distinguishing concurrent auditory objects.
The neural processes underlying concurrent sound segregation were examined by using event-related brain potentials. Participants were presented with complex sounds comprised of multiple harmonics,Expand
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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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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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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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Two-state folding observed in individual protein molecules.
The folding dynamics of small proteins are often described in terms of a simple two-state kinetic model. Within this notion, the behavior of individual molecules is expected to be stochastic, with aExpand
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Mapping protein collapse with single-molecule fluorescence and kinetic synchrotron radiation circular dichroism spectroscopy
We have used the combination of single-molecule Förster resonance energy transfer and kinetic synchrotron radiation circular dichroism experiments to probe the conformational ensemble of theExpand
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