Articles | Volume 20, issue 6
https://doi.org/10.5194/acp-20-3291-2020
© Author(s) 2020. This work is distributed under
the Creative Commons Attribution 4.0 License.
the Creative Commons Attribution 4.0 License.
https://doi.org/10.5194/acp-20-3291-2020
© Author(s) 2020. This work is distributed under
the Creative Commons Attribution 4.0 License.
the Creative Commons Attribution 4.0 License.
Research article
| 
20 Mar 2020
Research article |
| 20 Mar 2020
| 20 Mar 2020
Protein aggregates nucleate ice: the example of apoferritin
María Cascajo-Castresana
División de Salud, TECNALIA, Parque Tecnológico, Paseo de
Mikeletegi, 2, 20009 Donostia, Spain
CIC nanoGUNE, Tolosa Hiribidea, 76, 20018 Donostia, Spain
Department of Environmental System Sciences, Institute for Atmospheric
and Climate Science, ETH Zurich, 8092 Zurich, Switzerland
Robert O. David
Department of Environmental System Sciences, Institute for Atmospheric
and Climate Science, ETH Zurich, 8092 Zurich, Switzerland
Department of Geosciences, University of Oslo, Oslo, 0315, Norway
Maiara A. Iriarte-Alonso
CIC nanoGUNE, Tolosa Hiribidea, 76, 20018 Donostia, Spain
Alexander M. Bittner
CIC nanoGUNE, Tolosa Hiribidea, 76, 20018 Donostia, Spain
Ikerbasque, Basque Foundation for Science, Ma Díaz de Haro 3,
48013 Bilbao, Spain
Claudia Marcolli
CORRESPONDING AUTHOR
Department of Environmental System Sciences, Institute for Atmospheric
and Climate Science, ETH Zurich, 8092 Zurich, Switzerland
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- An experimentally representative in-silico protocol for dynamical studies of lyophilised and weakly hydrated amorphous proteins E. Bassotti et al. 10.1038/s42004-024-01167-6
- Cloud Activation via Formation of Water and Ice on Various Types of Porous Aerosol Particles E. Jantsch & T. Koop 10.1021/acsearthspacechem.0c00330
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- Effect of Aggregation and Molecular Size on the Ice Nucleation Efficiency of Proteins A. Alsante et al. 10.1021/acs.est.3c06835
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- Psychrophiles: A source of cold-adapted enzymes for energy efficient biotechnological industrial processes R. Bhatia et al. 10.1016/j.jece.2020.104607
- The ice–vapour interface during growth and sublimation M. Cascajo-Castresana et al. 10.5194/acp-21-18629-2021
- Comparing the ice nucleation properties of the kaolin minerals kaolinite and halloysite K. Klumpp et al. 10.5194/acp-23-1579-2023
- Microbial ice-binding structures: A review of their applications M. Uko et al. 10.1016/j.ijbiomac.2024.133670
- Inverse Relationship Between Ice Nucleation and Ice Growth Rates in Frozen Foods M. Zalazar et al. 10.1007/s11483-024-09881-3
- Ice Nucleation Ability of Tree Pollen Altered by Atmospheric Processing E. Gute et al. 10.1021/acsearthspacechem.0c00218
- Ice nucleation by viruses and their potential for cloud glaciation M. Adams et al. 10.5194/bg-18-4431-2021
- Electron microscopy and calorimetry of proteins in supercooled water J. Melillo et al. 10.1038/s41598-022-20430-1
- Metal Oxide Particles as Atmospheric Nuclei: Exploring the Role of Metal Speciation in Heterogeneous Efflorescence and Ice Nucleation Z. Schiffman et al. 10.1021/acsearthspacechem.2c00370
- Lignin's ability to nucleate ice via immersion freezing and its stability towards physicochemical treatments and atmospheric processing S. Bogler & N. Borduas-Dedekind 10.5194/acp-20-14509-2020
- Ultrafast Solar-Vapor Harvesting Based on a Hierarchical Porous Hydrogel with Wettability Contrast and Tailored Water States M. Yang et al. 10.1021/acsami.2c03597
- Structure and Protein-Protein Interactions of Ice Nucleation Proteins Drive Their Activity S. Hartmann et al. 10.3389/fmicb.2022.872306
26 citations as recorded by crossref.
- Insect Freeze-Tolerance Downunder: The Microbial Connection M. Morgan-Richards et al. 10.3390/insects14010089
- Atomic-Level Insights into a Unique Semi-Clathrate Hydrate Formed in a Confined Environment of Porous Protein Crystal B. Maity et al. 10.1021/acs.cgd.3c00880
- On the Vitality of the Classical Theory of Crystal Nucleation; Crystal Nucleation in Pure Own Melt; Atmospheric Ice and Snow; Ice in Frozen Foods C. Nanev 10.1016/j.pcrysgrow.2022.100567
- The presence of nanoparticles in aqueous droplets containing plant-derived biopolymers plays a role in heterogeneous ice nucleation P. Bieber et al. 10.1063/5.0213171
- Effect of viral infection on the ice nucleation efficiency of marine coccolithophores A. Alsante et al. 10.1080/02786826.2024.2420675
- Overview of biological ice nucleating particles in the atmosphere S. Huang et al. 10.1016/j.envint.2020.106197
- Ice nucleation catalyzed by the photosynthesis enzyme RuBisCO and other abundant biomolecules A. Alsante et al. 10.1038/s43247-023-00707-7
- Improving cryo-EM grids for amyloid fibrils using interface-active solutions and spectator proteins D. Valli et al. 10.1016/j.bpj.2024.02.009
- Ice nucleation in aqueous solutions of short- and long-chain poly(vinyl alcohol) studied with a droplet microfluidics setup L. Eickhoff et al. 10.1063/5.0136192
- The impact of (bio-)organic substances on the ice nucleation activity of the K-feldspar microcline in aqueous solutions K. Klumpp et al. 10.5194/acp-22-3655-2022
- An experimentally representative in-silico protocol for dynamical studies of lyophilised and weakly hydrated amorphous proteins E. Bassotti et al. 10.1038/s42004-024-01167-6
- Cloud Activation via Formation of Water and Ice on Various Types of Porous Aerosol Particles E. Jantsch & T. Koop 10.1021/acsearthspacechem.0c00330
- Production of ice-nucleating particles (INPs) by fast-growing phytoplankton D. Thornton et al. 10.5194/acp-23-12707-2023
- Effect of Aggregation and Molecular Size on the Ice Nucleation Efficiency of Proteins A. Alsante et al. 10.1021/acs.est.3c06835
- Ice nucleation activity of airborne pollen: A short review of results from laboratory experiments P. Duan et al. 10.1016/j.atmosres.2023.106659
- Psychrophiles: A source of cold-adapted enzymes for energy efficient biotechnological industrial processes R. Bhatia et al. 10.1016/j.jece.2020.104607
- The ice–vapour interface during growth and sublimation M. Cascajo-Castresana et al. 10.5194/acp-21-18629-2021
- Comparing the ice nucleation properties of the kaolin minerals kaolinite and halloysite K. Klumpp et al. 10.5194/acp-23-1579-2023
- Microbial ice-binding structures: A review of their applications M. Uko et al. 10.1016/j.ijbiomac.2024.133670
- Inverse Relationship Between Ice Nucleation and Ice Growth Rates in Frozen Foods M. Zalazar et al. 10.1007/s11483-024-09881-3
- Ice Nucleation Ability of Tree Pollen Altered by Atmospheric Processing E. Gute et al. 10.1021/acsearthspacechem.0c00218
- Ice nucleation by viruses and their potential for cloud glaciation M. Adams et al. 10.5194/bg-18-4431-2021
- Electron microscopy and calorimetry of proteins in supercooled water J. Melillo et al. 10.1038/s41598-022-20430-1
- Metal Oxide Particles as Atmospheric Nuclei: Exploring the Role of Metal Speciation in Heterogeneous Efflorescence and Ice Nucleation Z. Schiffman et al. 10.1021/acsearthspacechem.2c00370
- Lignin's ability to nucleate ice via immersion freezing and its stability towards physicochemical treatments and atmospheric processing S. Bogler & N. Borduas-Dedekind 10.5194/acp-20-14509-2020
- Ultrafast Solar-Vapor Harvesting Based on a Hierarchical Porous Hydrogel with Wettability Contrast and Tailored Water States M. Yang et al. 10.1021/acsami.2c03597
1 citations as recorded by crossref.
Latest update: 10 Dec 2024
Short summary
Atmospheric ice-nucleating particles are rare but relevant for cloud glaciation. A source of particles that nucleate ice above −15 °C is biological material including some proteins. Here we show that proteins of very diverse functions and structures can nucleate ice. Among these, the iron storage protein apoferritin stands out, with activity up to −4 °C. We show that its activity does not stem from correctly assembled proteins but from misfolded protein monomers or oligomers and aggregates.
Atmospheric ice-nucleating particles are rare but relevant for cloud glaciation. A source of...
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