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Updated: Aug 5, 2026

Microfluidic Mixers for Studying Protein Folding
Published on: April 10, 2012
Two state behavior in a solvable model of beta-hairpin folding
1Department of Physics, University of California, San Diego, 9500 Gilman Drive, La Jolla, California 92093-0319, USA.
Abstract:
Understanding the mechanism of protein secondary structure formation is an essential part of the protein-folding puzzle. Here we describe a simple model for the formation of a beta hairpin, motivated by the fact that folding of a beta hairpin captures much of the basic physics of protein folding. The modeled hairpin is composed of two interacting Gaussian chains with one pairwise (two-body) and two many-body interactions. We show that these many-body interactions, arising from side chain packing effects, are responsible for producing an "all-or-none" folding transition. We also estimate the (single exponential) folding/unfolding rate via calculating the thermodynamic weight of the "critical" droplet/bubble.
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