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Updated: Jul 19, 2026

Single-Molecule Measurement of Protein Interaction Dynamics Within Biomolecular Condensates
Published on: January 5, 2024
A simple semiempirical model for the effect of molecular confinement upon the rate of protein folding
Manajit Hayer-Hartl1, Allen P Minton
1Department of Cellular Biochemistry, Max Planck Institute for Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany.
Abstract:
A simple two-state model for the dependence of the rate of folding of a polypeptide confined within a spherical cavity upon the size of the cavity relative to that of the polypeptide is presented. A general prediction of the model is that decreasing the size of the cavity will increase the rate of refolding until the cavity becomes only slightly larger than the native state of the protein, at which point a further decrease in cavity size decreases the rate of refolding. The model qualitatively accounts for the behavior of several previously published simulations of folding within a cavity, as well as recently reported experimental measurements of the relative rate of refolding of each of five proteins encapsulated within wild-type and mutant GroEL-GroES complexes that have been engineered to provide internal cavities with similar surface composition and varying volume.
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