Abstract:
The similarity in the thermodynamic properties of two completely different theoretical models for the helix-coil transition is examined critically. The first model is an all-atomic representation for a poly-alanine chain, while the second model is a minimal helix-forming model that contains no system specifics. Key characteristics of the helix-coil transition, in particular, the effective critical exponents of these two models agree with each other, within a finite-size scaling analysis.
This is a preview of subscription content, access via your institution.
Author information
Authors and Affiliations
Additional information
Received 8 December 1999
Rights and permissions
About this article
Cite this article
Kemp, J., Hansmann, U. & Chen, Z. Is there a universality of the helix-coil transition in protein models?. Eur. Phys. J. B 15, 371–374 (2000). https://doi.org/10.1007/s100510051138
Issue Date:
DOI: https://doi.org/10.1007/s100510051138
- PACS. 87.15.He Dynamics and conformational changes - 87.15.-v Biomolecules: structure and physical properties - 64.60.Cn Order disorder transformations; statistical mechanics of model systems