Dresden 2014 – scientific programme
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BP: Fachverband Biologische Physik
BP 28: Protein structure and dynamics II
BP 28.2: Talk
Wednesday, April 2, 2014, 15:30–15:45, HÜL 386
Variable Temperature Single Molecule Force Spectroscopy of an Extremophilic Protein — •Katarzyna Tych1,2, Toni Hoffmann1,2, David Brockwell2, and Lorna Dougan1,2 — 1Molecular and Nanoscale Physics Group, School of Physics and Astronomy, University of Leeds, LS2 9JT, UK — 2Astbury Centre for Structural Molecular Biology and Institute of Molecular and Cellular Biology, University of Leeds, LS2 9JT, UK
Extremophiles (organisms which survive and thrive in the most extreme chemical and physical conditions on Earth) exhibit a range of fascinating cellular- and molecular-level adaptations. The flexibility of extremophilic proteins is one of the key determinants of their ability to function at the extremes of environmental temperatures.
We use single molecule force spectroscopy (SMFS) by atomic force microscopy (AFM) to measure the effect of temperature on the mechanical stability and flexibility of a protein derived from a hyperthermophilic organism.
The study was performed using an AFM SMFS instrument with variable temperature capabilities. We study temperature-dependent changes in the unfolding energy landscape of this protein by measuring changes in the unfolding force with temperature in combination with Monte Carlo simulations. We find that the position of the transition state to unfolding shifts away from the native state with increased temperature, reflecting a reduction in the spring constant of the protein and an increase in structural flexibility [1].
[1] K. M. Tych et al. (2013), Soft Matter (9): 9016-9025