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  Inhibition of Bacterial Ice Nucleators Is Not an Intrinsic Property of Antifreeze Proteins

Schwidetzky, R., Kunert, A. T., Bonn, M., Pöschl, U., Ramlov, H., DeVries, A. L., et al. (2020). Inhibition of Bacterial Ice Nucleators Is Not an Intrinsic Property of Antifreeze Proteins. The Journal of Physical Chemistry B, 124(24), 4889-4895. doi:10.1021/acs.jpcb.0c03001.

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Schwidetzky, Ralph1, Autor
Kunert, Anna T.2, Autor           
Bonn, Mischa1, Autor
Pöschl, Ulrich2, Autor           
Ramlov, Hans1, Autor
DeVries, Arthur L.1, Autor
Fröhlich-Nowoisky, Janine2, Autor           
Meister, Konrad1, Autor
Affiliations:
1external, ou_persistent22              
2Multiphase Chemistry, Max Planck Institute for Chemistry, Max Planck Society, ou_1826290              

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 Zusammenfassung: Cold-adapted organisms use antifreeze proteins (AFPs) or ice-nucleating proteins (INPs) for the survival in freezing habitats. AFPs have been reported to be able to inhibit the activity of INPs, a property that would be of great physiological relevance. The generality of this effect is not understood, and for the few known examples of INP inhibition by AFPs, the molecular mechanisms remain unclear. Here, we report a comprehensive evaluation of the effects of five different AFPs on the activity of bacterial ice nucleators using a high-throughput ice nucleation assay. We find that bacterial INPs are inhibited by certain AFPs, while others show no effect. Thus, the ability to inhibit the activity of INPs is not an intrinsic property of AFPs, and the interactions of INPs and different AFPs proceed through protein-specific rather than universal molecular mechanisms.

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Sprache(n): eng - English
 Datum: 2020-06-18
 Publikationsstatus: Erschienen
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 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: ISI: 000552403500003
DOI: 10.1021/acs.jpcb.0c03001
 Art des Abschluß: -

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Titel: The Journal of Physical Chemistry B
  Andere : J. Phys. Chem. B
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Washington, D.C. : American Chemical Society
Seiten: - Band / Heft: 124 (24) Artikelnummer: - Start- / Endseite: 4889 - 4895 Identifikator: ISSN: 1520-6106
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000293370_1