The antifreeze protein (AFP) activity is explained using two models. The first model is using ice binding and the second is using antiice
structuralization of water molecules. The description of AFP function using anti-ice structuralization of water molecules is less
explored. Therefore, it is of interest to explain AFP function using this model. Protein folding is often described using models where
hydrophobic residues move away from water getting buried and hydrophilic residues are exposed to the surface. Thus, the 3D Gauss
function stretched on the protein molecule describes the hydrophobicity distribution in a protein molecule. Small antifreeze proteins
(less than 150 residues) are often represented by structures with hydrophobic core. Large antifreeze proteins (above 200 residues)
contain solenoid (modular repeats). The hydrophobic field of solenoid show different distribution with linear propagation of the bands
of different hydrophobicity level having high and low hydrophobicity that is propagated parallel to the long axis of solenoid. This
specific ordering of hydrophobicity implies water molecules ordering different from ice. We illustrate this phenomenon using two antifreeze
proteins to describe the hypothesis.
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dc.subject.en
antifreeze protein
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dc.subject.en
models
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dc.subject.en
function
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dc.subject.en
activity
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dc.subject.en
ice
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dc.subject.en
anti-ice
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dc.description.volume
13
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dc.description.number
12
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dc.description.points
15
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dc.description.publication
0,25
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dc.identifier.doi
10.6026/97320630013400
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dc.identifier.eissn
0973-2063
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dc.title.journal
Bioinformation
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dc.language.container
eng
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dc.affiliation
Wydział Lekarski : Zakład Bioinformatyki i Telemedycyny
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dc.subtype
ReviewArticle
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dc.rights.original
CC-BY; otwarte czasopismo; ostateczna wersja wydawcy; w momencie opublikowania; 0