Berlin 2018 – wissenschaftliches Programm
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BP: Fachverband Biologische Physik
BP 12: Computational Biophysics I
BP 12.8: Vortrag
Dienstag, 13. März 2018, 11:45–12:00, H 1058
Loop formation of polyglutamines in the PRIME20 model — •Arne Böker and Wolfgang Paul — Martin-Luther-Universität Halle-Wittenberg, 06099 Halle
Much effort has recently been put into understanding amyloid formation in polypeptides. The amyloid state is an aggregated structure of polypeptides and usually differs from the native state. Amyloid formation can have various effects, beneficial as well as damaging, including diseases such as Huntington’s chorea, which is associated with an aggregated state of extended polyglutamine (polyQ) sequences. Loop structures or even β turns of single polyQ molecules may act as templates for aggregation, which motivates experimental investigation by energy transfer methods as well as our simulations.
We perform thermodynamic simulations of single polyQ chains represented by the intermediate-resolution PRIME20 model1 using the SAMC2 variation of Wang-Landau Monte Carlo sampling which provides insight into different statistical ensembles at the expense of dynamic information. Our results for the end-to-end distance distribution at physiological conditions agrees reasonably well with experimental findings. In this temperature range, the single-chain morphology for the chain lengths we studied is not yet dominated by hairpin structures which are formed at lower temperatures.
1M. Cheon, I. Chang, C. K. Hall, PROTEINS 78(2010):2950
2B. Werlich, T. Shakirov, M. P. Taylor, W. Paul, Comp. Phys. Comm. 186(2015):65