Related Experiment Video
Updated: Jul 18, 2026

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
Published on: April 28, 2011
Exact solution of the Muñoz-Eaton model for protein folding
Pierpaolo Bruscolini1, Alessandro Pelizzola
1Dipartimento di Fisica & INFM, Politecnico di Torino, c.so Duca degli Abruzzi 24, I-10129 Torino, Italy.
Abstract:
A transfer-matrix formalism is introduced to evaluate exactly the partition function of the Muñoz-Eaton model, relating the folding kinetics of proteins of known structure to their thermodynamics and topology. This technique can be used for a generic protein, for any choice of the energy and entropy parameters, and in principle allows the model to be used as a first tool to characterize the dynamics of a protein of known native state and equilibrium population. Applications to a beta-hairpin and to protein CI-2, with comparisons to previous results, are also shown.
Related Concept Videos
Protein Folding
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme can...
Protein Folding
Molecular Chaperones and Protein Folding
The...
Protein Organization
The primary structure of a protein is its amino acid sequence.
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

