Regensburg 2007 – scientific programme

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BP: Fachverband Biologische Physik

BP 4: Protein Structure and Folding

BP 4.3: Talk

Monday, March 26, 2007, 18:00–18:15, H43

Intrinsic structural properties of mesoscopic models for protein folding and aggregation — •Michael Bachmann^1,2, Stefan Schnabel¹, Christoph Junghans¹, and Wolfhard Janke¹ — ¹Institut für Theoretische Physik, Universität Leipzig, Augustusplatz 10/11, D-04109 Leipzig, Germany — ²Computational Biology & Biological Physics, Lunds Universitet, Sölvegatan 14A, SE-223 62 Lund, Sweden

In this talk, the importance of mesoscopic models for soft materials is illustrated for folding processes of protein-like heteropolymers [1] and their aggregation [2]. In addition, it is shown that the conformational transitions accompanying folding and aggregation processes of naturally finite systems are similar to phase transitions, but not in a strict thermodynamic sense. In particular, the aggregation studies reveal the advantages of a microcanonical analysis, compared to the standard canonical approach.

[1] S. Schnabel, M. Bachmann, and W. Janke, Phys. Rev. Lett., in print; J. Chem. Phys., in print.

[2] C. Junghans, M. Bachmann, and W. Janke, Phys. Rev. Lett. 97, 218103 (2006).