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The nucleic acid binding properties of the Cucumovirus RNAi suppressor tomato aspermy virus protein 2B (TAV 2B) are studied by using total internal reflection fluorescence spectroscopy (TIRFS). Binding to RNA has oligomerized and induced a conformational change in TAV 2B, causing it to form a primarily helical structure and a 4:2 protein-RNA complex.

A yellow fluorescent protein-MreB conjugate in merodiploid strain SC9 is used to study the behavior of MreB in Vibrio parahaemolyticus under various stresses, which could have significant implications for study of the cellular stress response and aging. The expression of MreB is declined in bacteria in the stationary phase and under starvation but is upregulated during the initial periods of cold shock and viable but nonculturable (VBNC) state differentiation.

A study was conducted to characterize the structural and dynamic properties of S2-HR2 which is one of the heptad repeat domains of the envelope glycoprotein from severe acute respiratory syndrome coronavirus (SARS-CoV). The results obtained for the transition state pathway of S2-HR2 from the prefusion state to the postfusion state might provide insights into the design of structure-based antagonists of SARS-CoV as well as other enveloped viruses.

A detailed high-resolution characterization of the membrane proximal external region (MPER) was performed to explore the structure-function relationship of glycoprotein (gp41) and its role in the HIV-1 fusion. The results obtained revealed that MPER stabilize the six-helix bundle (6-HB) and are participate in the interaction of T-20 (FUZEON, an anti-HIV-1 fusion inhibitor drug) with the gp41 fusion peptide proximal region (gp41 FP-PR).

The study presents a structural and dynamic characterization of the interaction that takes place between the putative fusion peptide of the S2 SARS coronavirus (SARS-CoV) virus protein and the lipid membranes. The putative fusion domain of SARS-CoV is shown to lead to the merging of the viral and target cell membranes.

The NMR structure of the W184A/M185A C-terminal domain (CTD) in its monomeric form is described. The studies have shown that dimerization-induced conformational changes are present in the two crystal structures of the CTD dimers and have suggested a mechanism that can accommodate both of the different dimer models playing functional roles during the Gag assembly of the immature capsids.

The stoichiometry of the newly developed NS3-NS5B oligomeric protein complex which could be used for treatment of liver diseases caused by Hepatitis C virus (HCV) is described.

Structural analysis of domain 2 of HCV NS5A (nonstructural protein 5A protein) (NS5A-D2) is conducted using multinuclear magnetic resonance spectroscopy. The results show that NS5A-D2 exists intrinsically unfolded but it still maintains in its functional state.

The proteomic studies conducted on all eukaryotic viruses and bacteriophages with regard to virion composition, viral protein structures, virus-virus and virus-host protein interactions and changes in the cellular proteome upon viral infection are discussed.

Research reveals that the membrane-proximal domain of the intact HIV-1 envelope is not involved in the membrane perturbations. It facilitates the bending of gp41 necessary for viral and target membranes fusion. Data show that the fusion gp41 fusion peptide, comprising the amino acid residues 665-683, is insufficient to cause HIV-1 envelope-mediated fusion.