M
Madeleine B. Borgia
Researcher at University of Zurich
Publications - 22
Citations - 1852
Madeleine B. Borgia is an academic researcher from University of Zurich. The author has contributed to research in topics: Intrinsically disordered proteins & Polyelectrolyte. The author has an hindex of 13, co-authored 17 publications receiving 1277 citations. Previous affiliations of Madeleine B. Borgia include University of Cambridge & St. Jude Children's Research Hospital.
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Journal ArticleDOI
Extreme disorder in an ultrahigh-affinity protein complex
Alessandro Borgia,Madeleine B. Borgia,Katrine Bugge,Vera M. Kissling,Pétur O. Heidarsson,Catarina B. Fernandes,Andrea Sottini,Andrea Soranno,Andrea Soranno,Karin J. Buholzer,Daniel Nettels,Birthe B. Kragelund,Robert B. Best,Benjamin Schuler +13 more
TL;DR: It is demonstrated the existence of an unexpected interaction mechanism: the two intrinsically disordered human proteins histone H1 and its nuclear chaperone prothymosin-α associate in a complex with picomolar affinity, but fully retain their structural disorder, long-range flexibility and highly dynamic character.
Journal ArticleDOI
Single-molecule spectroscopy reveals polymer effects of disordered proteins in crowded environments
Andrea Soranno,Iwo Koenig,Madeleine B. Borgia,Hagen Hofmann,Franziska Zosel,Daniel Nettels,Benjamin Schuler +6 more
TL;DR: Using single-molecule Förster resonance energy transfer, the effect of crowding as mimicked by commonly used biocompatible polymers is quantified and suggests that excluded volume interactions between overlapping biopolymers and the resulting criticality of the system can be essential contributions to the physics governing the crowded cellular milieu.
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Single-molecule fluorescence reveals sequence-specific misfolding in multidomain proteins
Madeleine B. Borgia,Alessandro Borgia,Robert B. Best,Annette Steward,Daniel Nettels,Bengt Wunderlich,Benjamin Schuler,Jane Clarke +7 more
TL;DR: It is inferred that the interactions underlying misfolding are very specific and result in a sequence-specific domain-swapping mechanism that is in excellent agreement with the observed transfer efficiency of the misfolded species.
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Consistent View of Polypeptide Chain Expansion in Chemical Denaturants from Multiple Experimental Methods.
Alessandro Borgia,Wenwei Zheng,Karin J. Buholzer,Madeleine B. Borgia,Anja Schüler,Hagen Hofmann,Andrea Soranno,Daniel Nettels,Klaus Gast,Alexander Grishaev,Robert B. Best,Benjamin Schuler +11 more
TL;DR: This is the first case in which SAXS and FRET have yielded even qualitatively consistent results regarding expansion in denaturant when applied to the same proteins, and this analysis demonstrates that both of these experimental probes are compatible with a common ensemble of protein configurations for eachDenaturant concentration.
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Temperature-dependent solvation modulates the dimensions of disordered proteins
René Wuttke,Hagen Hofmann,Daniel Nettels,Madeleine B. Borgia,Jeetain Mittal,Robert B. Best,Benjamin Schuler +6 more
TL;DR: This work uses single-molecule Förster resonance energy transfer to probe the temperature-induced chain collapse of five unfolded or intrinsically disordered proteins and finds that each of the proteins undergoes a collapse with increasing temperature, with the most hydrophobic one, λ-repressor, undergoing a reexpansion at the highest temperatures.