Regensburg 2019 – scientific programme
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BP: Fachverband Biologische Physik
BP 12: Poster II
BP 12.32: Poster
Tuesday, April 2, 2019, 14:00–16:00, Poster B2
Computer simulations of SAS-6 assembly on surfaces — •Dennis Wörthmüller1,2 and Ulrich Schwarz1,2 — 1Institute for Theoretical Physics, Heidelberg — 2Bioquant, Heidelberg
The scaffold protein SAS-6 self-assembles into a 9-fold ring that forms the structural basis for centrioles and thus is essential for many important cellular processes, including cell division and the genesis of cilia and flagella. Recently the self-assembly of SAS-6 has been studied by high-speed AFM on mica surfaces (Niervergelt et al., Nature Nanotechnology 13:696-701, 2018). Motivated by this experimental study, we have developed a 2D Brownian dynamics simulation model to identify possible assembly pathways, including malformed structures. Our main finding is that strong fluctuations, which are suppressed by the interaction with the surface, lead to malformed structures. Fluctuations also result in a distribution of ring sizes that favors 8-rings over 10-rings.