arXiv · 2010.12281
Linking thermodynamics and measurements of protein stability
Abstract
We review the background, theory and general equations for the analysis of equilibrium protein unfolding experiments, focusing on denaturant and heat-induced unfolding. The primary focus is on the thermodynamics of reversible folding/unfolding transitions and the experimental methods that are available for extracting thermodynamic parameters. We highlight the importance of modelling both how the folding equilibrium depends on a perturbing variable such as temperature or denaturant concentration, and the importance of modelling the baselines in the experimental observables.
Explore related subjects
Keep this discovery
Kresten Lindorff-Larsen, Kaare Teilum. 2020-10-23. Linking thermodynamics and measurements of protein stability. https://arxiv.org/abs/2010.12281
Cite the original work for its findings. Save a collection to share your selection of sources.