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Updated: Jul 16, 2026

Microfluidic Mixers for Studying Protein Folding
Published on: April 10, 2012
Two-state folding, folding through intermediates, and metastability in a minimalistic hydrophobic-polar model for
Stefan Schnabel1, Michael Bachmann, Wolfhard Janke
1Institut für Theoretische Physik and Centre for Theoretical Sciences (NTZ), Universität Leipzig, Augustusplatz 10/11, D-04109 Leipzig, Germany. Stefan.Schnabel@itp.uni-leipzig.de
Abstract:
Within the frame of an effective, coarse-grained hydrophobic-polar protein model, we employ multicanonical Monte Carlo simulations to investigate free-energy landscapes and folding channels of exemplified heteropolymer sequences, which are permutations of each other. Despite the simplicity of the model, the knowledge of the free-energy landscape in dependence of a suitable system order parameter enables us to reveal complex folding characteristics known from real bioproteins and synthetic peptides, such as two-state folding, folding through weakly stable intermediates, and glassy metastability.
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