Related Experiment Video
Updated: Jul 17, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
Published on: November 1, 2024
Internal protein dynamics shifts the distance to the mechanical transition state
Daniel K West1, Emanuele Paci, Peter D Olmsted
1School of Physics and Astronomy and School of Biochemistry and Microbiology, University of Leeds, Leeds LS2 9JT, United Kingdom.
Abstract:
Mechanical unfolding of polyproteins by force spectroscopy provides valuable insight into their free energy landscapes. Most experiments of the unfolding process have been fit to two-state and/or one dimensional models, with the details of the protein and its dynamics often subsumed into a zero-force unfolding rate and a distance x{u}{1D} to the transition state. We consider the entire phase space of a model protein under a constant force, and show that x{u}{1D} contains a sizeable contribution from exploring the full multidimensional energy landscape. This effect is greater for proteins with many degrees of freedom that are affected by force; and surprisingly, we predict that externally attached flexible linkers also contribute to the measured unfolding characteristics.
Related Concept Videos
Mechanical Protein Functions
Cooperative Allosteric Transitions
Cooperative Allosteric Transitions
Cooperative Allosteric Transitions
Energy to Drive Translocation
Generally, polypeptides are unfolded by two distinct...
Protein Diffusion in the Membrane

