https://doi.org/10.1007/s100510051138
Is there a universality of the helix-coil transition in protein models?
1
Department of Physics, University of Waterloo, Waterloo, Ontario, N2L 3G1, Canada
2
Department of Physics, Michigan Technological University, Houghton, MI 49931-1291, USA
Received:
8
December
1999
Published online: 15 May 2000
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.
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
© EDP Sciences, Società Italiana di Fisica, Springer-Verlag, 2000