Nanocrystallites Modulate Intermolecular Interactions in Cryoprotected Protein Solutions.
Journal
The journal of physical chemistry. B
ISSN: 1520-5207
Titre abrégé: J Phys Chem B
Pays: United States
ID NLM: 101157530
Informations de publication
Date de publication:
13 07 2023
13 07 2023
Historique:
medline:
14
7
2023
pubmed:
3
7
2023
entrez:
3
7
2023
Statut:
ppublish
Résumé
Studying protein interactions at low temperatures has important implications for optimizing cryostorage processes of biological tissue, food, and protein-based drugs. One of the major issues is related to the formation of ice nanocrystals, which can occur even in the presence of cryoprotectants and can lead to protein denaturation. The presence of ice nanocrystals in protein solutions poses several challenges since, contrary to microscopic ice crystals, they can be difficult to resolve and can complicate the interpretation of experimental data. Here, using a combination of small- and wide-angle X-ray scattering (SAXS and WAXS), we investigate the structural evolution of concentrated lysozyme solutions in a cryoprotected glycerol-water mixture from room temperature (
Identifiants
pubmed: 37399586
doi: 10.1021/acs.jpcb.3c02413
pmc: PMC10350957
doi:
Substances chimiques
Ice
0
Solvents
0
Solutions
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
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