This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Study of the virus assembly using high hydrostatic pressure and 2 photon fluorescence microscopy. Recent findings have emerged on the use of pressure to assess intermediate states of multimeric proteins, protein-nucleic acid complexes and in the assembly pathways of several viruses, in an effort to understand how the plasticity required for successful assembly is coded into the folded conformation of a capsid protein subunit. Interest in characterizing these states lies in the extent to which they can be related to genuine intermediates present in folding and assembly processes. Pressure effects can be monitored by using optical methods such as fluorescence spectroscopy. Using pressure to promote viral capsids dissociation, we have detected the presence of ribonucleoprotein intermediates, where the coat protein is partially unfolded but bound to RNA. These intermediates are potential targets for antiviral compounds. Since pressure can be used as a 'thermodynamic tweezer', its association with the FCS techniques will be a powerful tool to monitor the assembly and disassembly of virus capsids and to assess information on the possible intermediates involved in these processes.
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