Linking thermodynamics and measurements of protein stability
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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.
Originalsprog | Engelsk |
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Artikelnummer | gzab002 |
Tidsskrift | Protein engineering, design & selection : PEDS |
Vol/bind | 34 |
Antal sider | 13 |
ISSN | 1741-0126 |
DOI | |
Status | Udgivet - 2021 |
ID: 260744008