ArticleBeilstein journal of nanotechnology2022
Alcohol-perturbed self-assembly of the tobacco mosaic virus coat protein.
Article in Beilstein journal of nanotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 6 citations in OpenAlex.
- Extended Plasmonic Nanostructures Templated by Tobacco Mosaic Virus Coat Protein.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Design Principles Of Inorganic-Protein Hybrid Materials for Biomedicine.Exploration (Beijing, China) · 2025Review
- Innate Immune Response to Viral Infection.Advances in experimental medicine and biology · 2025Review
- Tunable Nanomaterials of Intracellular Crystallization for In Situ Biolabeling and Biomedical Imaging.Chemical & biomedical imaging · 2023Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The self-assembly of the tobacco mosaic virus coat protein is significantly altered in alcohol-water mixtures. Alcohol cosolvents stabilize the disk aggregate and prevent the formation of helical rods at low pH. A high alcohol content favours stacked disk assemblies and large rafts, while a low alcohol concentration favours individual disks and short stacks. These effects appear to be caused by the hydrophobicity of the alcohol additive, with isopropyl alcohol having the strongest effect and methanol the weakest. We discuss several effects that may contribute to preventing the protein-protein interactions between disks that are necessary to form helical rods.
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Registered trials
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