Monitoring protein unfolding transitions by NMR-spectroscopy.
Folding transition
Global unfolding
NMR exchange regime
Protein folding
Journal
Journal of biomolecular NMR
ISSN: 1573-5001
Titre abrégé: J Biomol NMR
Pays: Netherlands
ID NLM: 9110829
Informations de publication
Date de publication:
Apr 2022
Apr 2022
Historique:
received:
21
10
2021
accepted:
28
12
2021
pubmed:
6
1
2022
medline:
22
4
2022
entrez:
5
1
2022
Statut:
ppublish
Résumé
NMR-spectroscopy has certain unique advantages for recording unfolding transitions of proteins compared e.g. to optical methods. It enables per-residue monitoring and separate detection of the folded and unfolded state as well as possible equilibrium intermediates. This allows a detailed view on the state and cooperativity of folding of the protein of interest and the correct interpretation of subsequent experiments. Here we summarize in detail practical and theoretical aspects of such experiments. Certain pitfalls can be avoided, and meaningful simplification can be made during the analysis. Especially a good understanding of the NMR exchange regime and relaxation properties of the system of interest is beneficial. We show by a global analysis of signals of the folded and unfolded state of GB1 how accurate values of unfolding can be extracted and what limits different NMR detection and unfolding methods. E.g. commonly used exchangeable amides can lead to a systematic under determination of the thermodynamic protein stability. We give several perspectives of how to deal with more complex proteins and how the knowledge about protein stability at residue resolution helps to understand protein properties under crowding conditions, during phase separation and under high pressure.
Identifiants
pubmed: 34984658
doi: 10.1007/s10858-021-00389-3
pii: 10.1007/s10858-021-00389-3
pmc: PMC9018662
doi:
Substances chimiques
Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
3-15Informations de copyright
© 2022. The Author(s).
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