Document 
Eur. Phys. J. B 15, 371-374
Is there a universality of the helix-coil transition in protein models?
J.P. Kemp1 - U.H.E. Hansmann2 - Zheng Yu Chen1
1 Department of Physics, University of Waterloo, Waterloo, Ontario, N2L 3G1, Canada
2 Department of Physics, Michigan Technological University, Houghton, MI 49931-1291, USA
hansmann@mtu.edu
Received 8 December 1999
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.
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
Copyright EDP Sciences, Società Italiana di Fisica, Springer-Verlag