Restricted reactivity of the iε-amino groups of tobacco mosaic virus protein toward trinitrobenzenesulfonic acid

Biochemistry ◽  
1969 ◽  
Vol 8 (9) ◽  
pp. 3597-3603 ◽  
Author(s):  
Robert B. Scheele ◽  
Max A. Lauffer
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Virus Protein ◽  
Amino Groups ◽  
Trinitrobenzenesulfonic Acid

scholarly journals THE PARTIAL REACTIVATION OF FORMOLIZED TOBACCO MOSAIC VIRUS PROTEIN

1938 ◽  
Vol 22 (2) ◽  
pp. 165-191 ◽  
Author(s):  
A. Frank Ross ◽  
W. M. Stanley
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Amino Nitrogen ◽  
Specific Property ◽  
Virus Protein ◽  
Amino Groups ◽  
Reactivation Process ◽  
Virus Activity ◽  
Simultaneous Decrease ◽  
Phenol Reagent

A marked reactivation of tobacco mosaic virus protein that has been partially or completely inactivated by formaldehyde was obtained by dialysis at pH 3. The activity of partially inactivated virus proteins was generally increased about 10-fold by the reactivation process. It was also found possible to reactivate completely inactive preparations to an appreciable extent. It was shown that the inactivation and the subsequent reactivation cannot be explained by the toxicity of the formaldehyde or of the formolized protein or by aggregation. Inactivation was accompanied by a decrease in amino groups as indicated by Van Slyke gasometric determinations and by colorimetric estimations using ninhydrin. Inactivation also causes a decrease in the number of groups that react with Folin's reagent at pH 7.7. The latter are probably the indole nuclei of tryptophane, for it was demonstrated that tryptophane, glycyltryptophane, and indole propionic acid react with formaldehyde in a similar manner, while tyrosine and glycyltyrosine do not. Evidence that reactivation is accompanied by an increase in amino nitrogen and in groups that react with Folin's reagent was obtained by colorimetric estimation. The demonstration that the addition of formaldehyde to the virus protein results in a simultaneous decrease of activity, of amino groups, and of groups that react with Folin's phenol reagent, and that under conditions favorable for the removal of formaldehyde the virus activity is regained and the number of such groups increases, indicates that certain of these groups play at least a partial role in the structure necessary for virus activity. These changes can best be interpreted on the basis of known chemical reactions and are considered as evidence that virus activity is a specific property of the protein.

Three-dimensional reconstruction of the stacked-disk aggregate of tobacco mosaic virus protein from electron micrographs

1971 ◽  
Vol 261 (837) ◽  
pp. 211-219 ◽  
Keyword(s):  
Electron Microscope ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Virus Protein ◽  
Protein Subunits ◽  
Microscope Images ◽  
Dimensional Reconstruction ◽  
Inner Parts

The three-dimensional structure of the stacked-disk rod of tobacco mosaic virus protein has been reconstructed to a resolution of about 2 nm from electron microscope images. Closed rings of seventeen protein subunits (compared with 16 ⅓ in one turn of the virus helix) are stacked in polar fashion, the stacking being accompanied by an axial perturbation of periodicity 5.3 nm connecting successive pairs of rings into disks. The axial perturbation consists of a movement towards each other of the outer parts of the subunits in the two rings comprising a disk, together with a movement of the inner parts in the opposite direction. This could be explained either by a bending of parts of the subunits in the appropriate directions or by a bodily tilting of the subunits in the two rings in opposite directions.

In vitro and in vivo aggregation of the defective PM2 tobacco mosaic virus protein

1966 ◽  
Vol 19 (1) ◽  
pp. 140-IN8 ◽  
Author(s):  
Albert Siegel ◽  
G.J. Hills ◽  
Roy Markham
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Virus Protein
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