ABSTRACT
This presentation is not about grammar. Rather, it presents a quite different viewpoint on how to approach scientific writing. Central to this approach is the consideration that scientific writing is persuasive, narrative writing. I will present how this viewpoint can be used by authors to better present their data and interpretations of their data to readers. This approach facilitates writing to reader’s expectations. I will provide a blueprint on how to tackle the task.

ABSTRACT
Since the discovery of superoxide dismutase in 1968, the research on free radicals and related oxidants has had as a primary focus the chemistry of these species and the damage they can induce in cells and tissues. In 1980 we proposed that these species could be signalling molecules for major cell events such as cell division and differentiation. In the last decade the research community has come to realize the central role that redox biochemistry in determining the biology of the cell. Free radicals, related oxidants (e.g. H2O2), and antioxidant enzymes dictate this redox biology. In this presentation I expand on our work that links superoxide, hydrogen peroxide, and the superoxide/peroxide-removing system to the basic biology of the cell. I will present new ideas on the differing roles that superoxide, hydrogen peroxide, and antioxidants enzymes have in the basic redox biology of the cell. For a primer, see: Free Radic Biol Med. 41: 1338-1350, 2006 and Free Radic Biol Med. 30: 1191-1212, 2001.

ABSTRACT
An exciting new general method will be described that makes it possible to genetically encode unnatural amino acids into proteins to endow them with diverse physical, chemical, or biological properties. The method has been successfully implemented in a variety of species including Escherichia coli, yeast, and mammalian cells. More than 30 unnatural amino acids have been incorporated into proteins with high fidelity and efficiency by means of a unique codon and corresponding tRNA/aminoacyl-tRNA synthetase pair. These include fluorescent, glycosylated, metal-ion-binding, and redox-active amino acids, as well as amino acids with unique chemical and photochemical reactivity. This methodology provides a powerful tool both for exploring protein structure and function in vitro and in vivo, and for generating proteins with new or enhanced properties.

ABSTRACT
The complement system is an integral participant in the innate mechanisms of immunity and thus has a burden of performing surveillance in the host and protect it from all the pathogens including viruses. It has been shown that both acute and latent viruses are susceptible to complement-mediated neutralization. Thus, complement exerts a strong selective pressure on viruses during infection. These data suggest that for their successful survival, viruses must have developed mechanisms to subvert this system. Consistent with this premise, genome sequencing of poxviruses and herpesviruses have shown that members of these families encode for structural homologs of human regulators of the complement activation (RCA) family. Using expressed proteins, we have shown that these viruses encode functional regulators of complement. The mechanism by which these proteins modulate complement activation and their in vivo functioning will be presented.

ABSTRACT
The correlation between protein structure and function is well established yet the role flexibility plays in protein function is currently being explored. We have developed an in vivo screen in which the thermal stability and flexibility of a test protein is directly correlated to the transcriptional regulation of a reporter gene. The system entails the use of an engineered 3-domain construct where the N- and C-terminal domains are constant and the central domain is variable. When the central domain is highly flexible the reporter gene is up-regulated to a greater extent relative to more stable variants. Mutant variants of the G1 domain were used to benchmark the in vivo screen and spectroscopic methods were employed to characterize the thermal and structural properties of each variant. The screen was also combined with in silico methods to interrogate a library of randomized variants for selection of mutants of greater structural integrity.