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Updated: Jul 7, 2026

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
Published on: April 28, 2011
Thermodynamics and kinetics of a Gō proteinlike heteropolymer model with two-state folding characteristics
Anna Kallias1, Michael Bachmann, Wolfhard Janke
1Institut für Theoretische Physik, Universität Leipzig, Postfach 100 920, D-04009 Leipzig, Germany and Centre for Theoretical Sciences (NTZ), Universität Leipzig, Postfach 100 920, D-04009 Leipzig, Germany.
Abstract:
We present results of Monte Carlo computer simulations of a coarse-grained hydrophobic-polar Gō-like heteropolymer model and discuss thermodynamic properties and kinetics of an exemplified heteropolymer, exhibiting two-state folding behavior. It turns out that general, characteristic folding features of realistic proteins with a single free-energy barrier can also be observed in this simplified model, where the folding transition is primarily driven by the hydrophobic force.
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