Journal ArticleDOI
Polymerization of tobacco mosaic virus protein and its control.
A. C. H. Durham,Aaron Klug +1 more
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Near neutral pH9 TMV protein sub-units polymerize into two-layer aggregates culminating in the 20S disk, whereas the helical rod forms cooperatively at acid pH, controlled by the state of ions of two abnormally titrating carboxyl groups.Abstract:
Near neutral pH9 TMV protein sub-units polymerize into two-layer aggregates culminating in the 20S disk, whereas the helical rod forms cooperatively at acid pH. The mode of aggregation is controlled by the state of ionization of two abnormally titrating carboxyl groups.read more
Citations
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Journal ArticleDOI
Supramolecular Polymers in Aqueous Media
TL;DR: This review discusses one-dimensional supramolecular polymers that form in aqueous media and focuses on recent studies that address key challenges in the field, providing mechanistic understanding, rational polymer design, important functionality, robustness, or unusual thermodynamic and kinetic properties.
Journal ArticleDOI
The tobacco mosaic virus particle: structure and assembly
TL;DR: A short account is given of the physical and chemical studies that have led to an understanding of the structure of the tobacco mosaic virus particle and how it is assembled from its constituent coat protein and RNA.
Journal ArticleDOI
Movement and self-control in protein assemblies. Quasi-equivalence revisited.
TL;DR: A mechanical model of the contractile T4 tail sheath has been constructed to demonstrate how self-controlled activation of a latent bonding potential can drive a purposeful movement.
Journal ArticleDOI
States of aggregation of tobacco mosaic virus protein.
TL;DR: Self-assembly of the protein subunits of tobacco mosaic virus takes place by a series of steps and control of the aggregation and its consequences for virus assembly are described in the next two articles.
Journal ArticleDOI
Assembly of the particle of tobacco mosaic virus from RNA and disks of protein.
P.J.G. Butler,Aaron Klug +1 more
TL;DR: The reconstitution of TMV does not proceed by the stepwise addition of single protein subunits, but by the addition of preformed disks to the growing rod, which is the basis of the selectivity for viral over other RNAs.
References
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Book ChapterDOI
Assembly and Stability of the Tobacco Mosaic Virus Particle
TL;DR: The structural and physical chemical studies on TMV considered in this chapter provide a picture of the way in which the viral nucleic acid is packaged for transmission, and illustrate some general principles regarding the molecular organization of biological structures.
Journal ArticleDOI
States of aggregation of tobacco mosaic virus protein.
TL;DR: Self-assembly of the protein subunits of tobacco mosaic virus takes place by a series of steps and control of the aggregation and its consequences for virus assembly are described in the next two articles.
Journal ArticleDOI
Assembly of the particle of tobacco mosaic virus from RNA and disks of protein.
P.J.G. Butler,Aaron Klug +1 more
TL;DR: The reconstitution of TMV does not proceed by the stepwise addition of single protein subunits, but by the addition of preformed disks to the growing rod, which is the basis of the selectivity for viral over other RNAs.
Book ChapterDOI
Structure of the tobacco mosaic virus particle; polymerization of tobacco mosaic virus protein.
TL;DR: A critical analysis of the molecular weight of tobacco mosaic virus (TMV) and with polymerization of TMV protein is described and the correctness of the assumption that water is released upon polymerization is established.
Journal ArticleDOI
The use of negative staining in the electron microscopic examination of plant viruses in crude extracts.
J.H. Hitchborn,G.J. Hills +1 more
TL;DR: Careful examination was necessary to detect particles of the viruses of cucumber mosaic, lucerne mosaic, tobacco necrosis, and tobacco ringspot, either because few particles were present or because they were poorly contrasted against the background.