PubMed · 5823266
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L Levi. 1969-07-26. Automatic gain control model for vision.. https://doi.org/10.1038/223396b0
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An analytic model of the ultrasonic modulation of multiply scattered coherent light in scattering media is developed based on two mechanisms: the ultrasonic modulation of the index of refraction and the ultrasonic modulation of the displacements of Rayleigh scatterers. In water solutions, for example, the first mechanism is slightly less important than the second mechanism when the scattering mean free path is less than a critical fraction (0.0890) of the acoustic wavelength, and it becomes increasingly more important beyond this point. This model agrees well with an independent Monte Carlo model.
Amino acid sequences of nucleocapsid proteins are mostly conserved among different rhabdoviruses. The protein plays a common functional role in different RNA viruses by enwrapping the viral genomic RNA in an RNase-resistant form. Upon expression of the nucleocapsid protein alone in COS cells and in bacteria, it forms large insoluble aggregates. In this work, we have reported for the first time the full-length cloning of the N gene of Chandipura virus and its expression in Escherichia coli in a soluble monomeric form and purification using nonionic detergents. The biological activity of the soluble recombinant protein has been tested, and it was found to possess efficient RNA-binding ability. The state of aggregation of the recombinant protein was monitored using light scattering. In the absence of nonionic detergents, it formed large aggregates. Aggregation was significantly reduced in the presence of osmolytes such as d-sorbitol. Aggregate formation was suppressed in the presence of another viral product, phosphoprotein P, in a chaperone-like manner. Both the osmolyte and phosphoprotein P also suppressed aggregation to a great extent during refolding from a guanidine hydrochloride-denatured form. The function of the phosphoprotein and osmolyte appears to be synergistic to keep the N-protein in a soluble biologically competent form in virus-infected cells.