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Updated: Aug 6, 2026

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
Published on: April 28, 2011
Glassy dynamics of side-chain ordering in a simple model of protein folding
Edo Kussell1, Eugene I Shakhnovich
1Department of Biophysics, Harvard University, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.
Abstract:
We introduce a modified version of protein lattice models in which monomers have several spin states, representing side-chain rotamers. Completion of folding corresponds to reaching the native backbone configuration with complete ordering of side chains. We find that as temperature is lowered, side-chain ordering becomes much slower than backbone folding. The presence of side chains leads to nonexponential kinetics and a broad distribution of relaxation times.
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