Berlin 2008 – scientific programme

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BP: Fachverband Biologische Physik

BP 25: Protein Structure and Folding

BP 25.4: Talk

Thursday, February 28, 2008, 15:15–15:30, PC 203

Thermodynamics and kinetics of a protein-like heteropolymer model with two-state folding characteristics — Anna Kallias, •Michael Bachmann, and Wolfhard Janke — Institut für Theoretische Physik, Universität Leipzig, Postfach 100 920, D-04009 Leipzig

We present results of Monte Carlo computer simulations of a coarse-grained hydrophobic-polar Gō-like heteropolymer model and discuss thermodynamic properties and kinetics of an exemplified heteropolymer, exhibiting two-state folding behavior [1]. We find that thermodynamic and kinetic properties as, for example, the folding temperature within this model, are quantitatively consistent. It turns out that general, characteristic folding features of realistic proteins with a single free-energy barrier can also be observed in this simplified model, where the folding transition is primarily driven by the hydrophobic force. As further recent results [2], our study shows that characteristic features of protein folding are intrinsic properties of heteropolymers and thus even observable on mesoscopic scales.

[1] A. Kallias, M. Bachmann, and W. Janke, J. Chem. Phys., in print (2007).

[2] S. Schnabel, M. Bachmann, and W. Janke, Phys. Rev. Lett. 98, 048103 (2007).