ArticleBMC structural biology2011
Novel dimeric β-helical model of an ice nucleation protein with bridged active sites.
Article in BMC structural biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 136 citations in OpenAlex.
- A previously unrecognized class of fungal ice-nucleating proteins with bacterial ancestry.Science advances · 2026Article
- Protein Confinement Decouples Dynamical Heterogeneity from Structural Preordering in Supercooled Monolayer Water.JACS Au · 2025Article
- Leveraging structure-informed machine learning for fast steric zipper propensity prediction across whole proteomes.PLoS computational biology · 2025Article
- Hierarchical assembly and environmental enhancement of bacterial ice nucleators.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Measuring the Surface Tension of Atmospheric Particles and Relevant Mixtures to Better Understand Key Atmospheric Processes.Chemical reviews · 2024Review
- Improving cryo-EM grids for amyloid fibrils using interface-active solutions and spectator proteins.Biophysical journal · 2024Article
- Effect of Aggregation and Molecular Size on the Ice Nucleation Efficiency of Proteins.Environmental science & technology · 2024Article
- Surface-displayed silicatein-α enzyme in bioengineeredFrontiers in systems biology · 2024Article
- Ice nucleation proteins self-assemble into large fibres to trigger freezing at near 0 °C.eLife · 2023Article
- Functional aggregation of cell-free proteins enables fungal ice nucleation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Ice nucleation proteins self-assemble into large fibres to trigger freezing at near 0 °C.bioRxiv : the preprint server for biology · 2023Article
- Electron microscopy and calorimetry of proteins in supercooled water.Scientific reports · 2022Article
- Article
- Water-organizing motif continuity is critical for potent ice nucleation protein activity.Nature communications · 2022Article
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- Toward Understanding Bacterial Ice Nucleation.The journal of physical chemistry. B · 2022Article
- Structure and Protein-Protein Interactions of Ice Nucleation Proteins Drive Their Activity.Frontiers in microbiology · 2022Article
- Regulated strategies of cold-adapted microorganisms in response to cold: a review.Environmental science and pollution research international · 2021Review
- Specific Ion-Protein Interactions Influence Bacterial Ice Nucleation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- A Microfluidic Device for Automated High Throughput Detection of Ice Nucleation of SnomaxMicromachines · 2021Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
backgroundIce nucleation proteins (INPs) allow water to freeze at high subzero temperatures. Due to their large size (>120 kDa), membrane association, and tendency to aggregate, an experimentally-determined tertiary structure of an INP has yet to be reported. How they function at the molecular level therefore remains unknown.
resultsHere we have predicted a novel β-helical fold for the INP produced by the bacterium Pseudomonas borealis. The protein uses internal serine and glutamine ladders for stabilization and is predicted to dimerize via the burying of a solvent-exposed tyrosine ladder to make an intimate hydrophobic contact along the dimerization interface. The manner in which PbINP dimerizes also allows for its multimerization, which could explain the aggregation-dependence of INP activity. Both sides of the PbINP structure have tandem arrays of amino acids that can organize waters into the ice-like clathrate structures seen on antifreeze proteins.
conclusionsDimerization dramatically increases the 'ice-active' surface area of the protein by doubling its width, increasing its length, and presenting identical ice-forming surfaces on both sides of the protein. We suggest that this allows sufficient anchored clathrate waters to align on the INP surface to nucleate freezing. As PbINP is highly similar to all known bacterial INPs, we predict its fold and mechanism of action will apply to these other INPs.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.