Berlin 2015 – scientific programme

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BP: Fachverband Biologische Physik

BP 52: Protein structure and dynamics II

BP 52.6: Talk

Friday, March 20, 2015, 11:15–11:30, H 1028

Exploring the multiscale signaling behavior of phototropin1 from Chlamydomonas reinhardtii using a full-residue space kinetic Monte Carlo molecular dynamics technique — Emanuel Peter, Bernhard Dick, Ivan Stambolic, and •Stephan Baeurle — Institut für Physikalische und Theoretische Chemie, Universität Regensburg, 93040 Regensburg

Devising analysis tools for elucidating the regulatory mechanism of complex enzymes has been a challenging task for many decades. It generally requires the determination of the structural-dynamic information of protein solvent systems far from equilibrium over multiple length and time scales, which is still difficult both theoretically and experimentally. To cope with the problem, we introduce a full-residue space multiscale simulation method [1] based on a combination of the kinetic Monte Carlo and molecular dynamics techniques, in which the rates of the rate-determining processes are evaluated from a biomolecular forcefield on the fly during the simulation run by taking into account the full space of residues. To demonstrate its reliability and efficiency, we explore the light-induced functional behavior of the full-length phototropin1 from Chlamydomonas reinhardtii (Cr-phot1). Our results demonstrate that in the signaling state the kinase is activated through the disruption of the Jalpha-helix from the light-oxygen-voltage-2-sensitive (LOV2) domain, which is followed by a stretching of the activation loop and broadening of the catalytic cleft of the kinase. Literature: [1] E. Peter, B. Dick, I. Stambolic, S.A. Baeurle, Prot. Struct. Funct. Bioinf. 82, 2018 (2014).