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Updated: Jun 17, 2026

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
Published on: April 28, 2011
A statistical approach to the estimation of mechanical unfolding parameters from the unfolding patterns of protein
1School of Chemistry, University of Leeds, Leeds, LS2 9JT, UK. G.S.Beddard@chem.leeds.ac.uk
Abstract:
A statistical calculation is described with which the saw-tooth-like unfolding patterns of concatenated heteropolymeric proteins can be used to estimate the forced unfolding parameters of a previously uncharacterized protein. The chance of observing the various sequences of unfolding events, such as ABAABBB or BBAAABB etc, for two proteins of types A and B is calculated using proteins with various ratios of A and B and at different values of effective unfolding rate constants. If the experimental rate constant for forced unfolding, k(0), and distance to the transition state x(u) are known for one protein, then the calculation allows an estimation of values for the other. The predictions are compared with Monte Carlo simulations and experimental data.
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