Interfacial Water Ordering Is Insufficient to Explain Ice-Nucleating Protein Activity.


Journal

The journal of physical chemistry letters
ISSN: 1948-7185
Titre abrégé: J Phys Chem Lett
Pays: United States
ID NLM: 101526034

Informations de publication

Date de publication:
14 Jan 2021
Historique:
pubmed: 17 12 2020
medline: 23 1 2021
entrez: 16 12 2020
Statut: ppublish

Résumé

Ice-nucleating proteins (INPs) found in bacteria are the most effective ice nucleators known, enabling the crystallization of water at temperatures close to 0 °C. Although their function has been known for decades, the underlying mechanism is still under debate. Here, we show that INPs from

Identifiants

pubmed: 33326244
doi: 10.1021/acs.jpclett.0c03163
doi:

Substances chimiques

Bacterial Outer Membrane Proteins 0
ice nucleation protein 0
Water 059QF0KO0R

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

218-223

Auteurs

Max Lukas (M)

Max Planck Institute for Polymer Research, 55128 Mainz, Germany.

Ralph Schwidetzky (R)

Max Planck Institute for Polymer Research, 55128 Mainz, Germany.

Anna T Kunert (AT)

Max Planck Institute for Chemistry, 55128 Mainz, Germany.

Ellen H G Backus (EHG)

Max Planck Institute for Polymer Research, 55128 Mainz, Germany.
Department of Physical Chemistry, University of Vienna, 1090 Vienna, Austria.

Ulrich Pöschl (U)

Max Planck Institute for Chemistry, 55128 Mainz, Germany.

Janine Fröhlich-Nowoisky (J)

Max Planck Institute for Chemistry, 55128 Mainz, Germany.

Mischa Bonn (M)

Max Planck Institute for Polymer Research, 55128 Mainz, Germany.

Konrad Meister (K)

Max Planck Institute for Polymer Research, 55128 Mainz, Germany.
University of Alaska Southeast, Juneau, Alaska 99801, United States.

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Classifications MeSH