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Single-Molecule Spectroscopy of Intrinsically Disordered Proteins and Their Interaction Mechanisms

CMCB Green Seminar

Date:25.10.2018, 16:00 - 17:00
Speaker: Ben Schuler, University of Zurich, Institute of Biochemistry
Location: CRTD, auditorium left
Host: Michael Schlierf / James Saenz

Abstract
The functions of proteins have traditionally been linked to their well-defined three-dimensional, folded structures. It is becoming increasingly clear, however, that many proteins perform essential functions without being folded. Single-molecule spectroscopy provides new opportunities for investigating the structure, dynamics, and interaction mechanisms of such unfolded or 'intrinsically disordered' proteins (IDPs). I will focus on a recent example of two IDPs that bind one another with very high affinity yet remain unstructured. This type of interaction has interesting ramifications for kinetic mechanisms of binding and cellular regulation.

5 most recent papers
Borgia, A., Borgia, M., Bugge, K., Kissling, V.M., Heidarsson, P.O., Fernandes, C.B., Sottini, A., Soranno, A., Buholzer, K., Nettels, D., Kragelund, B.B., Best, R.B., & Schuler, B. (2018) Extreme disorder in an ultra-high-affinity protein complex. Nature, 555, 61-66.

Zosel, F., Mercadante, D., Nettels, D. & Schuler, B. (2018) A proline switch explains kinetic heterogeneity in a coupled folding and binding reaction. Nat. Comm. 9:3332

Soranno, A., Holla, A., Dingfelder, F., Nettels, D., Makarov, D.E. & Schuler, B. (2017) Integrated view of internal friction in unfolded proteins from single-molecule FRET, contact quenching, theory, and simulations. Proc. Natl. Acad. Sci. USA 114, E1833-E1839.

Schuler, B. (2018) Perspective: Chain dynamics of unfolded and intrinsically disordered proteins from nanosecond fluorescence correlation spectroscopy combined with single-molecule FRET. J. Chem. Phys. 149, 010901

Schuler, B., Hofmann, H., Nettels, D. & Soranno, A. (2016) Single-molecule FRET spectroscopy and the polymer physics of unfolded and intrinsically disordered proteins. Annu. Rev. Biophys. 45, 207-231.

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