Linking thermodynamics and measurements of protein stability.
Journal
Protein engineering, design & selection : PEDS
ISSN: 1741-0134
Titre abrégé: Protein Eng Des Sel
Pays: England
ID NLM: 101186484
Informations de publication
Date de publication:
15 02 2021
15 02 2021
Historique:
received:
23
10
2020
revised:
21
12
2020
accepted:
12
01
2021
entrez:
16
3
2021
pubmed:
17
3
2021
medline:
29
10
2021
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 33724431
pii: 6173616
doi: 10.1093/protein/gzab002
pii:
doi:
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
© The Author(s) 2021. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.