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- Publications
- Influence
Consistent View of Polypeptide Chain Expansion in Chemical Denaturants from Multiple Experimental Methods.
- A. Borgia, Wenwei Zheng, +9 authors B. Schuler
- Chemistry, Medicine
- Journal of the American Chemical Society
- 1 September 2016
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 techniques… Expand
Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopy
- H. Hofmann, Andrea Soranno, A. Borgia, K. Gast, D. Nettels, B. Schuler
- Chemistry, Medicine
- Proceedings of the National Academy of Sciences
- 14 September 2012
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
Single-molecule spectroscopy reveals polymer effects of disordered proteins in crowded environments
- Andrea Soranno, I. Koenig, +4 authors Benjamin Schuler
- Chemistry, Medicine
- Proceedings of the National Academy of Sciences
- 17 March 2014
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 known… Expand
Quantifying internal friction in unfolded and intrinsically disordered proteins with single-molecule spectroscopy
- Andrea Soranno, Brigitte Buchli, +7 authors B. Schuler
- Chemistry, Medicine
- Proceedings of the National Academy of Sciences
- 6 April 2012
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
Ultrafast dynamics of protein collapse from single-molecule photon statistics
- D. Nettels, I. Gopich, A. Hoffmann, B. Schuler
- Chemistry, Medicine
- Proceedings of the National Academy of Sciences
- 20 February 2007
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 occurs… Expand
Extreme disorder in an ultrahigh-affinity protein complex
- A. Borgia, Madeleine B Borgia, +10 authors B. Schuler
- Medicine
- Nature
- 1 March 2018
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 precise… Expand
Single-molecule fluorescence reveals sequence-specific misfolding in multidomain proteins
- Madeleine B Borgia, A. Borgia, +5 authors J. Clarke
- Biology, Medicine
- Nature
- 29 May 2011
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 cent… Expand
Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein
- R. Kellner, H. Hofmann, Alessandro Barducci, Bengt Wunderlich, D. Nettels, B. Schuler
- Chemistry, Medicine
- Proceedings of the National Academy of Sciences
- 27 August 2014
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… Expand
Charge interactions can dominate the dimensions of intrinsically disordered proteins
- S. Müller-Späth, Andrea Soranno, +5 authors B. Schuler
- Chemistry, Medicine
- Proceedings of the National Academy of Sciences
- 16 July 2010
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) often… Expand
Charge interactions can dominate the dimensions of intrinsically disordered proteins
- S. Müller-Späth, Andrea Soranno, +7 authors B. Schuler
- Chemistry
- 17 August 2010
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) often… Expand