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Updated: Jul 7, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Thermodynamics of peptide aggregation processes: an analysis from perspectives of three statistical ensembles
Christoph Junghans1, Michael Bachmann, Wolfhard Janke
1Institut für Theoretische Physik and Centre for Theoretical Sciences NTZ, Universität Leipzig, Postfach 100920, D-04009 Leipzig, Germany. junghans@mpip.mainz.mpg.de
Abstract:
We employ a mesoscopic model for studying aggregation processes of proteinlike hydrophobic-polar heteropolymers. By means of multicanonical Monte Carlo computer simulations, we find strong indications that peptide aggregation is a phase separation process, in which the microcanonical entropy exhibits a convex intruder due to non-negligible surface effects of the small systems. We analyze thermodynamic properties of the conformational transitions accompanying the aggregation process from the multicanonical, canonical, and microcanonical perspective. It turns out that the microcanonical description is particularly advantageous as it allows for unraveling details of the phase-separation transition in the thermodynamic region, where the temperature is not a suitable external control parameter anymore.
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