ArticleComputational and structural biotechnology journal2021
Molecular basis of ice-binding and cryopreservation activities of type III antifreeze proteins.
Article in Computational and structural biotechnology journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 17 citations in OpenAlex.
- The Study of Ice-Binding Protein Oligomeric Complexes.International journal of molecular sciences · 2025Article
- Protein Is an Intelligent Micelle.Entropy (Basel, Switzerland) · 2023Article
- Nanoscopy of single antifreeze proteins reveals that reversible ice binding is sufficient for ice recrystallization inhibition but not thermal hysteresis.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
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8 authors at 4 institutions in 1 country.
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Abstract
Antifreeze proteins (AFPs) can inhibit the freezing of body fluid at subzero temperatures to promote the survival of various organisms living in polar regions. Type III AFPs are categorized into three subgroups, QAE1, QAE2, and SP isoforms, based on differences in their isoelectric points. We determined the thermal hysteresis (TH), ice recrystallization inhibition (IRI), and cryopreservation activity of three isoforms of the notched-fin eelpout AFP and their mutant constructs and characterized their structural and dynamic features using NMR. The QAE1 isoform is the most active among the three classes of III AFP isoforms, and the mutants of inactive QAE2 and SP isoforms, QAE2
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