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DY: Fachverband Dynamik und Statistische Physik

DY 7: Poster I

DY 7.8: Poster

Montag, 11. März 2013, 17:30–19:30, Poster C

Structure optimization for models of protein folding by means of “local heat pulse”-quench cycles — •Florian Günther¹, Arnulf Möbius², and Michael Schreiber¹ — ¹Institute of Physics, Chemnitz University of Technology, Chemnitz, Germany — ²Institute for Theoretical Solid State Physics, IFW, Dresden, Germany

Protein folding is a very challenging task because the energy landscape exhibits a huge number of local minima. For such simulations, efficient heuristic algorithms are of high value. We investigate, whether and how the “local heat pulse”-quench cycling (LHPQC) approach [1], which has proved to be highly efficient for traveling salesman and Coulomb glass problems, can be applied to protein folding tasks. For that, we consider the hydrophobic-polar lattice model [2] and the continuous “3-color, 46-bead” model [3]. In evaluating the efficiency of the LHPQC approach, we compare with standard procedures as simulated annealing.

[1] A. Möbius, A. Neklioudov, A. Diaz-Sanchez, K.H. Hoffmann, A. Fachat, and M. Schreiber, Phys. Rev. Lett. 79 (1997) 4297.

[2] K. F. Lau, and K. A. Dill, Macromolecules 22 (1989) 3986.

[3] J. D. Honeycutt, and D. Thirumalai, Proc. Natl. Acad. Sci. USA 87 (1990) 3526.