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Is there a universality of the helix-coil transition in protein models?

2000/03/07 by Josh P. Kemp, J.P. Kemp, Ulrich H. E. Hansmann +3 · 1 citation
Biochemistry, Genetics and Molecular Biology · Chemistry · Materials Science · Physics and Astronomy · #Advanced Physical and Chemical Molecular Interactions #Enzyme Structure and Function #Protein Structure and Dynamics #cond-mat.stat-mech #physics.chem-ph #q-bio

paper · pdf · doi:10.1007/s100510051138

Latex, to appear in Eur. Phys. J. B

arxiv created 2000/03/07 · openalex publication_date 2000/05/01 · arxiv updated 2009/11/30 · openalex created_date 2016/06/24 · openalex updated_date 2026/08/01

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.

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