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Updated: Sep 4, 2026

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
Published on: April 28, 2011
Thermal folding and mechanical unfolding pathways of protein secondary structures
Marek Cieplak1, Trinh Xuan Hoang, Mark O Robbins
1Department of Physics and Astronomy, The Johns Hopkins University, Baltimore, Maryland, USA. mc@ifpan.edu.pl
Abstract:
Mechanical stretching of secondary structures is studied through molecular dynamics simulations of a Go-like model. Force versus displacement curves are studied as a function of the stiffness and velocity of the pulling device. The succession of stretching events, as measured by the order in which contacts are ruptured, is compared to the sequencing of events during thermal folding and unfolding. Opposite cross-correlations are found for an alpha-helix and a beta-hairpin structure. In a tandem of two alpha-helices, the two constituent helices unravel nearly simultaneously. A simple condition for simultaneous versus sequential unraveling of repeat units is presented.
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