title: Microcanonical analyses of peptide aggregation processes.
abstract: We propose the use of microcanonical analyses for numerical studies of peptide aggregation transitions. Performing multicanonical Monte Carlo simulations of a simple hydrophobic-polar continuum model for interacting heteropolymers of finite length, we find that the microcanonical entropy behaves convex in the transition region, leading to a negative microcanonical specific heat. As this effect is also seen in first-order-like transitions of other finite systems, our results provide clear evidence for recent hints that the characterization of phase separation in first-order-like transitions of finite systems profits from this microcanonical view.
authors.affiliation: Institut für Theoretische Physik and Centre for Theoretical Sciences (NTZ), Universität Leipzig, Augustusplatz 10/11, D-04109 Leipzig, Germany. Christoph.Junghans@itp.uni-leipzig.de
authors.forename: Christoph
authors.initials: C
authors.lastname: Junghans
authors.forename: Michael
authors.initials: M
authors.lastname: Bachmann
authors.forename: Wolfhard
authors.initials: W
authors.lastname: Janke
mesh_terms: D055598:Chemical Phenomena; D002627:Chemistry, Physical; D019277:Entropy; D057927:Hydrophobic and Hydrophilic Interactions; D009010:Monte Carlo Method; D046912:Multiprotein Complexes; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding; D013816:Thermodynamics
chemical_list: D046912:Multiprotein Complexes; D010455:Peptides