Why do antifreeze proteins require a solenoid?

2018
journal article
article
27
cris.lastimport.wos2024-04-09T19:05:16Z
dc.abstract.enProteins whose presence prevents water from freezing in living organisms at temperatures below 0 C are referred to as antifreeze proteins. This group includes molecules of varying size (from 30 to over 300 aa) and variable secondary/supersecondary conformation. Some of these proteins also contain peculiar structural motifs called solenoids. We have applied the fuzzy oil drop model in the analysis of four categories of antifreeze proteins: 1 e very small proteins, i.e. helical peptides (below 40 aa); 2 e small globular proteins (40e100 aa); 3 e large globular proteins (>100 aa) and 4 e proteins containing solenoids. The FOD model suggests a mechanism by which antifreeze proteins prevent freezing. In accordance with this theory, the presence of the protein itself produces an ordering of water molecules which counteracts the formation of ice crystals. This conclusion is supported by analysis of the ordering of hydrophobic and hydrophilic residues in antifreeze proteins, revealing significant variability e from perfect adherence to the fuzzy oil drop model through structures which lack a clearly defined hydrophobic core, all the way to linear arrangement of alternating local minima and maxima propagating along the principal axis of the solenoid (much like in amyloids). The presented model e alternative with respect to the ice docking model e explains the antifreeze properties of compounds such as saccharides and fatty acids. The fuzzy oil drop model also enables differentiation between amyloids and antifreeze proteins.pl
dc.affiliationWydział Lekarski : Zakład Bioinformatyki i Telemedycynypl
dc.cm.date2020-01-07
dc.cm.id85947
dc.contributor.authorBanach, Mateusz - 103003 pl
dc.contributor.authorKonieczny, Leszekpl
dc.contributor.authorRoterman-Konieczna, Irena - 133298 pl
dc.date.accessioned2020-01-17T09:19:00Z
dc.date.available2020-01-17T09:19:00Z
dc.date.issued2018pl
dc.date.openaccess0
dc.description.accesstimew momencie opublikowania
dc.description.physical74-84pl
dc.description.points30pl
dc.description.versionostateczna wersja wydawcy
dc.description.volume144pl
dc.identifier.doi10.1016/j.biochi.2017.10.011pl
dc.identifier.eissn1638-6183pl
dc.identifier.issn0300-9084pl
dc.identifier.projectROD UJ / OPpl
dc.identifier.urihttps://ruj.uj.edu.pl/xmlui/handle/item/141708
dc.languageengpl
dc.language.containerengpl
dc.rightsUdzielam licencji. Uznanie autorstwa - Użycie niekomercyjne - Bez utworów zależnych 4.0 Międzynarodowa*
dc.rights.licenceCC-BY-NC-ND
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/legalcode.pl*
dc.share.typeinne
dc.subject.enhydrophobicitypl
dc.subject.enantifreeze proteinspl
dc.subject.ensolenoidpl
dc.subject.enamyloidpl
dc.subtypeArticlepl
dc.titleWhy do antifreeze proteins require a solenoid?pl
dc.title.journalBiochimiepl
dc.typeJournalArticlepl
dspace.entity.typePublication
cris.lastimport.wos
2024-04-09T19:05:16Z
dc.abstract.enpl
Proteins whose presence prevents water from freezing in living organisms at temperatures below 0 C are referred to as antifreeze proteins. This group includes molecules of varying size (from 30 to over 300 aa) and variable secondary/supersecondary conformation. Some of these proteins also contain peculiar structural motifs called solenoids. We have applied the fuzzy oil drop model in the analysis of four categories of antifreeze proteins: 1 e very small proteins, i.e. helical peptides (below 40 aa); 2 e small globular proteins (40e100 aa); 3 e large globular proteins (>100 aa) and 4 e proteins containing solenoids. The FOD model suggests a mechanism by which antifreeze proteins prevent freezing. In accordance with this theory, the presence of the protein itself produces an ordering of water molecules which counteracts the formation of ice crystals. This conclusion is supported by analysis of the ordering of hydrophobic and hydrophilic residues in antifreeze proteins, revealing significant variability e from perfect adherence to the fuzzy oil drop model through structures which lack a clearly defined hydrophobic core, all the way to linear arrangement of alternating local minima and maxima propagating along the principal axis of the solenoid (much like in amyloids). The presented model e alternative with respect to the ice docking model e explains the antifreeze properties of compounds such as saccharides and fatty acids. The fuzzy oil drop model also enables differentiation between amyloids and antifreeze proteins.
dc.affiliationpl
Wydział Lekarski : Zakład Bioinformatyki i Telemedycyny
dc.cm.date
2020-01-07
dc.cm.id
85947
dc.contributor.authorpl
Banach, Mateusz - 103003
dc.contributor.authorpl
Konieczny, Leszek
dc.contributor.authorpl
Roterman-Konieczna, Irena - 133298
dc.date.accessioned
2020-01-17T09:19:00Z
dc.date.available
2020-01-17T09:19:00Z
dc.date.issuedpl
2018
dc.date.openaccess
0
dc.description.accesstime
w momencie opublikowania
dc.description.physicalpl
74-84
dc.description.pointspl
30
dc.description.version
ostateczna wersja wydawcy
dc.description.volumepl
144
dc.identifier.doipl
10.1016/j.biochi.2017.10.011
dc.identifier.eissnpl
1638-6183
dc.identifier.issnpl
0300-9084
dc.identifier.projectpl
ROD UJ / OP
dc.identifier.uri
https://ruj.uj.edu.pl/xmlui/handle/item/141708
dc.languagepl
eng
dc.language.containerpl
eng
dc.rights*
Udzielam licencji. Uznanie autorstwa - Użycie niekomercyjne - Bez utworów zależnych 4.0 Międzynarodowa
dc.rights.licence
CC-BY-NC-ND
dc.rights.uri*
http://creativecommons.org/licenses/by-nc-nd/4.0/legalcode.pl
dc.share.type
inne
dc.subject.enpl
hydrophobicity
dc.subject.enpl
antifreeze proteins
dc.subject.enpl
solenoid
dc.subject.enpl
amyloid
dc.subtypepl
Article
dc.titlepl
Why do antifreeze proteins require a solenoid?
dc.title.journalpl
Biochimie
dc.typepl
JournalArticle
dspace.entity.type
Publication
Affiliations

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