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 interacting with these substrate proteins in different ways. However, it has remained a challenge to measure the cha...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2014-09, Vol.111 (37), p.13355-13360
Hauptverfasser:	Kellner, Ruth, Hofmann, Hagen, Barducci, Alessandro, Wunderlich, Bengt, Nettels, Daniel, Schuler, Benjamin
Format:	Artikel
Sprache:	eng
Schlagworte:	Aggregation Binding Sites Biological Sciences Computer Simulation Escherichia coli - metabolism Escherichia coli Proteins - metabolism Fluorescence Histograms HSP40 Heat-Shock Proteins - metabolism HSP70 Heat-Shock Proteins - metabolism Kinetics Lead Microfluidics Models, Molecular Molecular chaperones Molecular Chaperones - metabolism Molecules polypeptides Protein Denaturation Protein folding Protein refolding Proteins Simulation Spectrometry, Fluorescence - methods Spectroscopy Spectrum analysis Substrate Specificity Thiosulfate Sulfurtransferase - metabolism
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