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Updated: May 30, 2026

Microfluidic Mixers for Studying Protein Folding
Published on: April 10, 2012
A new two-state polymer folding model and its application to α-helical polyalanine
Per Linse1, Peter Palenčár, Tomáš Bleha
1Physical Chemistry, Department of Chemistry, Lund University, Box 124, SE-221 00 Lund, Sweden. per.linse@fkem1.lu.se
Abstract:
A new two-state polymer folding model is proposed, in which the folding of a stiff helical polymer is enabled by allowing for short sequences of coils connecting shorter and separated helices. The folding is driven by short-range attraction energy among stacked helices and is opposed by the free-energy cost of forming coils from helical monomers. Principal outcomes of the model are equilibrium distribution of the number of helices and their length in helical polymers. The proposed model is applied to α-helical polyalanine. The distribution of the number of α-helices as a function of number of alanine residues is fitted to the corresponding result from molecular dynamics simulation employing an all-atom potential model with very good agreement. The influence and significance of the fitting parameters and possible use of the two-state folding model are discussed.
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