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BP: Fachverband Biologische Physik

BP 35: Posters: Statistical Physics, Evolution, and Networks

BP 35.7: Poster

Donnerstag, 25. März 2010, 17:15–20:00, Poster B2

Effect of thermostating and electrostatics on the solution structure and dynamics of signal transduction of the wildtype-LOV1 domain of phototropin — Emanuel Peter, Bernhard Dick, and •Stephan Baeurle — Institut für Physikalische und Theoretische Chemie, Universität Regensburg, Universitätsstr. 31, 93053 Regensburg, Deutschland

Phototropins are photoactive proteins in plants and algae, which consist of 2 LOV-(light oxygen voltage sensitive)-domains and 1 kinase domain. Each LOV-domain contains a noncovalently bound flavin-mononucleotid-(FMN)-chromophor, which after absorption of blue light at around 450 nm undergoes a photoreaction with a cysteine-residue attached to an apoprotein, inducing a signal in the organism via the kinase-domain. Both the signal transduction as well as the mechanism of the photoreaction of these domains are still only poorly understood. In this presentation we show results of molecular dynamics simulations, where we investigated the effect of thermostating and long-range electrostatics on the solution structure and dynamics of signal transduction of the wildtype LOV1-domain of the green algae Chlamydomonas rheinhardtii. By comparing our calculation results with recent simulation and experimental data, we demonstrate that these issues have an important influence on the equilibrium structure and the time-evolution of the system.