Abstract
We compare two recently proposed methods for the characterization of phase transitions in small systems. The usefulness of these techniques is evaluated for the case of structural transition in alanine-based peptides.
Highlights
When phase transitions are studied in statistical physics, the basic assumption is usually that the dimensions of the macroscopic system are very large compared with that of the constituting elements
In this paper we try to evaluate the usefulness and validity of the Borrmann et al and the Janke and Kenna (JK) approaches for the investigation of structural transitions in biomolecules, another important example for “phase transitions” in small systems
Analyzing the partition function zeros for this peptide, we find a “phase transition” at two temperatures, each being characterized by a line of complex zeros
Summary
When phase transitions are studied in statistical physics, the basic assumption is usually that the dimensions of the macroscopic system are very large compared with that of the constituting elements. The main question is how the observed effects in small systems can be related to true phase transitions in macroscopic (or infinite) systems. Attempts in this direction include the exploration of the density of complex zeros of the canonical partition function for finite and small systems by Borrmann et al [2] and the linear behavior for this limiting density [3, 4]. In this paper we try to evaluate the usefulness and validity of the Borrmann et al and the JK approaches for the investigation of structural transitions in biomolecules, another important example for “phase transitions” in small systems. We investigate a second molecule Ala10-Gly5-Ala in the context of Borrmann et al approach
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