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BP: Fachverband Biologische Physik
BP 14: Posters: Protein Structure and dynamics
BP 14.2: Poster
Dienstag, 1. April 2014, 09:30–12:30, P1
A multiscale model for fibrinogen — •Stephan Köhler1,2, Martin McCullagh3, Friederike Schmid1, and Giovanni Settanni1,4 — 1Institut für Physik, Johannes Gutenberg-Universität Mainz, Mainz, Germany — 2Graduate School Materials Science in Mainz — 3Department of Chemistry and Institute for Biophysical Dynamics, University of Chicago, Chicago, Illinois, United States — 4Max Planck Graduate Center mit der Johannes Gutenberg-Universität Mainz
The blood protein fibrinogen (fg) plays an important role in the coagulation cascade and the immune response to injury. However, these functions may also be initiated by fg aggregation on extraneous bodies such as, e.g. medical implants. In our previous work, atomistic molecular dynamics simulations have been used to characterize fg flexibility in solution [1]. Due to the size of the protein complex, however, atomistic simulation of fg aggregates at surfaces are not possible with current computers. Lower resolution models are required to address these systems. Here we present a new coarse grained (CG) model for fg that systematically incorporates data from all atom molecular dynamics simulations. This model reduces the resolution from nearly 31000 interacting particles in an all atom model to 45 CG beads.A heterogeneous elastic network connecting the beads is able to capture the dynamics on large and intermediate scales while the charges assigned to the coarse grained beads elucidate the charge structure of fibrinogen.
[1] Fibrinogen flexibilty and adsorption properties investigated using atomistic molecular dynamics simulations - S. Köhler, F. Schmid and G. Settanni, DPG meeting '14 abstract BP205