Ice recrystallization is strongly inhibited when antifreeze proteins bind to multiple ice planes.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
13 02 2019
13 02 2019
Historique:
received:
07
08
2018
accepted:
23
11
2018
entrez:
15
2
2019
pubmed:
15
2
2019
medline:
26
8
2020
Statut:
epublish
Résumé
Ice recrystallization is a phenomenon observed as the increase in ice crystal size within an already frozen material. Antifreeze proteins (AFPs), a class of proteins capable of arresting ice crystal growth, are known to inhibit this phenomenon even at sub milli-molar concentrations. A tremendous range in the possible applications of AFPs is hence expected in both medical and industrial fields, while a key determinant of the ice recrystallization inhibition (IRI) is hardly understood. Here, IRI efficiency and ice plane affinity were examined for the wild-type AFPI-III, a defective AFPIII isoform, and a fungal AFP isoform. To simplify the IRI analysis using the formal representation of Ostwald-ripening (r
Identifiants
pubmed: 30760774
doi: 10.1038/s41598-018-36546-2
pii: 10.1038/s41598-018-36546-2
pmc: PMC6374469
doi:
Substances chimiques
Antifreeze Proteins
0
Ice
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2212Références
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