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Humboldt-Universität zu Berlin - IRI Life Sciences

Humboldt-Universität zu Berlin | IRI Life Sciences | Events | Tutorials | Past events | Tutorial in Life Sciences - Ben Schuler: "Single-Molecule Spectroscopy of Protein Folding Dynamics"

Tutorial in Life Sciences - Ben Schuler: "Single-Molecule Spectroscopy of Protein Folding Dynamics"

  • Past
  • Tutorial
When Feb 28, 2016 from 02:00 PM to 05:00 PM (Europe/Vienna / UTC100) iCal
Where Phillipstr.13, Haus 18, Maud Menten Hall

Ben Schuler

University of Zurich


The spontaneous self-organization of an unstructured polypeptide into a well-defined three-dimensional structure is one of the most fundamental processes of life, and its complexity poses one of the central challenges for experimental and theoretical biophysics. Single-molecule spectroscopy has emerged as a versatile approach for investigating the structure, dynamics, and folding of proteins on a wide range of time scales and even in complex environments, including live cells.

The tutorial will first cover the basic methodological aspects of single-molecule spectroscopy, with a focus on dynamic and structurally heterogeneous systems. The combination of Förster resonance energy transfer (FRET) with nanosecond correlation spectroscopy, microfluidic mixing, and a detailed analysis of the complete photon statistics, including fluorescence lifetimes and anisotropies, provides distance information on timescales from nanoseconds to hours – essentially the entire range of timescales relevant for folding processes. These methods will then be illustrated with recent advances in the field. A starting point will be the sub-microsecond dynamics of unfolded proteins, which can be conceptualized in the framework of polymer physics and have important implications for the theoretical description of protein folding and the functional properties of the growing class of “intrinsically disordered proteins”. Single molecule spectroscopy can also be used to investigate the folding and dynamics of proteins in more complex environments, e.g. in the context of cellular factors, such as molecular chaperones, or to investigate the role of protein assembly and misfolding.Both the underlying conceptual questions and the methodological developments that have been crucial to address them will be discussed.