Quasi-elastic behavior of solutions of viral capsid and RNA at very low shearing stresses.
By the application of shearing stresses on the order of 10(-3) dyne cm-2 (10(-2) muN cm-2), via the magnetic viscodensimeter, extremely high relative viscosities (greater than 500) were observed when turnip yellow mosaic virus was degraded in alkali into its capsid and RNA. The solutions, however, possessed a watery consistency at this stage and exhibited a quasi-elastic character by rotor-recoil experiments. The development of this curious behavior was concentration and temperature dependent; it was not seen less than 0.5% nor at 8 degrees, and appeared sooner at 30 degrees than at 20 degrees. The time of appearance was delayed as the pH was lowered; however, the effect was still observed when the pH was as low as 9. Whereas reversibility was demonstrated when the shearing stresses exceeded the elastic resistance [0.17 dyne cm-2 (1.7 muN CM-2)], thorough mixing usually resulted in a normal behavior of the solutions thereafter. Values for the modulus of rigidity at 20 degrees for about 1% virus concentration was less than 2 X 10(-2) dyne cm-2 rad-1 (0.2 muN cm-2 rad-1), which, while extremely small, was reproducible. A porous structure, possibly involving a capsid and RNA complex, is envisioned.
D009029:Mosaic Viruses; D010942:Plant Viruses; D012367:RNA, Viral; D012996:Solutions; D013696:Temperature; D014764:Viral Proteins; D014783:Viscosity
D012367:RNA, Viral; D012996:Solutions; D014764:Viral Proteins