Related Experiment Video
Updated: Mar 30, 2026

Measuring Biomolecular DSC Profiles with Thermolabile Ligands to Rapidly Characterize Folding and Binding Interactions
Published on: November 21, 2017
Molecular Dynamics Simulations of the Temperature Induced Unfolding of Crambin Follow the Arrhenius Equation
Andrew Dalby1, Mohd Shahir Shamsir2
1Faculty of Science and Technology, University of Westminster, London, W1W 6UW, UK.
Abstract:
Molecular dynamics simulations have been used extensively to model the folding and unfolding of proteins. The rates of folding and unfolding should follow the Arrhenius equation over a limited range of temperatures. This study shows that molecular dynamic simulations of the unfolding of crambin between 500K and 560K do follow the Arrhenius equation. They also show that while there is a large amount of variation between the simulations the average values for the rate show a very high degree of correlation.
Related Concept Videos
Molecular Chaperones and Protein Folding
The...
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR
Protein Folding
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

