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Harold Boone is the Product R&D Director for The Dow Elastomers & Polymer Processing R&D group with capabilities located in Lake Jackson, TX, and Shanghai, China.  He is responsible for the development of a broad innovation portfolio focused on new olefin elastomer products and technologies.    Harold joined Dow as an organic polymer chemist in 1996 in Dow’s Central Research investigating thermally stable perfluoroaryl ether polymers for interlayer dielectrics and fundamental studies of polar monomer interactions with olefin polymerization catalysts.  Harold has held several sci

Glycosylation is a post-translational modification that affects cellular adhesion and host-pathogen interactions, with changes occurring during differentiation, immune response, and in cancerous tissue. Though as much as 70% of the proteome is glycosylated, determining the structure of these modifications is difficult. My research involves the expression and analysis of glycoproteins to develop a molecular understanding of how glycan heterogeneity and structure affect glycoprotein function.

Dr Gonen is an expert in electron crystallography and cryo EM. He determined the 1.9Å resolution structure of the water channel aquaporin-0 by electron crystallography, the highest resolution for any protein determined by cryo EM techniques at the time. Dr Gonen established his own laboratory at the University of Washington in 2005 together with the very first cryo EM laboratory in the Pacific Northwest, a resource that continues to benefit many researchers at the UW School of Medicine and beyond.

Abstract: Living, chain-growth methods for synthesizing conjugated polymers have the potential to access to new materials with varying sequences, lengths and end-groups. We recently used these methods to synthesize conjugated materials with random, block and gradient sequences of a poly(3-hexylthiophene) (P3HT) backbone and side-chain fullerenes (PC61BM). These polymers were evaluated as compatibilizers in photovoltaic devices with P3HT:PC61BM as the active layer.

Dr. Meanwell has led drug discovery programs in the cardiovascular, neurosciences and virology therapeutic areas, work that has resulted in the advancement of over 30 clinical candidates for the prevention of thrombosis, the treatment of stroke and therapy for viral infections, including human immunodeficiency virus-1 (HIV-1), hepatitis C virus (HCV) and respiratory syncytial virus (RSV).

Research in the Taylor Lab:

Protein phosphorylation is critical for regulation in eukaryotic cells. The human genome encodes more than 500 protein kinases, making this one of the largest gene families. Although very diverse in how they receive and transmit signals, all protein kinases share a conserved catalytic core. While it is essential to understand how these enzymes function as catalysts, it is equally important to understand how they are regulated, how they function as scaffolds, and how they are localized.

Heavy metal ions are typically considered to be detrimental to human health and are therefore considered to be a nuisance in both industrial and medicinal settings. The proper control of these ions via chelation, however, can engender them with beneficial applications in both regards. In this talk, I will discuss our group’s efforts to design chelators for heavy metal ions spanning the s-, d-, and f-block. We will show how unusual thermodynamic binding affinities can be obtained via ligand design efforts.

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