LMP Seminar (video conference): Nanoscale Brownian Dynamics of Semiflexible Biopolymers

LMP Seminar (video conference)

  • Datum: 22.09.2020
  • Uhrzeit: 14:00 - 15:30
  • Vortragende(r): Dr. Steffen Mühle
  • University of Göttingen
  • Ort: Max-Planck-Institut für Dynamik und Selbstorganisation (MPIDS)
  • Raum: Link to the talk: https://zoom.us/j/96266444298
  • Gastgeber: MPIDS / LMP
  • Kontakt: evelyn.tang@ds.mpg.de
While the theoretical foundations for describing molecular motion can be traced back more than a century, experimental techniques allowing us to measure the dynamics of single molecules have only become available in the last twenty years. Here, we aim to link the two together and use data from single-molecule experiments to infer characteristic properties of individual proteins in a systematic and quantitative manner. In particular, we have at our disposal three complementing methods which measure dynamical properties of single molecules. The first is photo-induced electron transfer paired with fluorescence correlation spectroscopy (PET-FCS) which measures their end-to-end or internal-to-end loop formation rate, the second is dual-focus fluorescence correlation spectroscopy (2fFCS) which measures their hydrodynamic radius, and the third is dynamic metal-induced energy transfer (dynaMIET) which measures their reconfiguration time when bound to a surface. In this talk, a custom polymer model which enables the efficient interpretation of results from PET-FCS, 2fFCS and dynaMIET experiments is presented. This model is a bead-rod chain which takes into account hydrodynamic interactions, excluded volume effects, bending rigidity and the fluorophore with which the protein is labeled, while including only two free parameters. It quantitatively reproduces systematically measured data from PET-FCS and 2fFCS applied to glycine-serine (GS) repeats – the prototype of an intrinsically disordered protein (IDP). Loop formation dynamics in GS-repeats typically take tens of nanoseconds, and their hydrodynamic radius is around one nanometer. From this data, the model yields a persistence length of lP=5.2+-1.9 Å and one amino acid’s hydrodynamic radius of a=3.5+-0.7 Å. Thus, we now have at hand a combined method of performing single-molecule experiments and Brownian dynamics simulations for IDPs which yields quantitative insights into their molecular properties.
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