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All Seminars are at 3:40PM in PSH151, unless otherwise stated.

David C. Muddiman 

Department of Chemistry
North Carolina State University   

Innovative Chemistries and Technologies to Read the Complex Language of Biology


Mass spectrometry offers the most robust platform to discover and characterize biological species across all molecular classes, including xenobiotics. We developed bioanalytical tools to characterize structurally challenging analytes that are critical to a systems-level analysis. To increase the electrospray response of N-linked glycans, we synthesized novel hydrophobic tagging reagents which have the added benefit of being able to incorporate a stable-isotope label for relative quantification experiments (INLIGHTTM). Furthermore, we developed a novel ionization technique for tissue imaging of lipids, metabolites, and bioactive peptides (IR-MALDESI). These innovative strategies will be presented in the context of ovarian cancer and treatment and adherence of HIV drugs.


Host: Jia Guo


Arjan van der Vaart 

University of South Florida  Department of Chemistry 

Host: Jeff Yarger and Marcia Levitus


Yi Lu 

University of Illinois  Department of Chemistry 

Design and Selection of Metalloenzymes and their Applications as Biocatalysts in Alternative Energies and as Biosensors in Environmental Monitoring, Medical Diagnostics and Imaging

Host: Jeremy Mills


Metalloenzymes play important roles in numerous biological processes. Designing metalloenzymes is an ultimate test of our knowledge about metalloenzymes and can result in new biocatalysts for practical applications such as in alternatives energies. We have been focusing ways to design heteronuclear metalloenzymes involved in multiple electron redox processes, such as heme-copper oxidase, heme-non-hem iron nitric oxide reductase and heme-[4Fe4S] cluster sulfite reductase. In the process, we demonstrate, while reproducing the primary coordination sphere may be good enough to make structural models of metalloproteins, careful design of the non-covalent secondary coordination sphere interactions, such as hydrophobicity and hydrogen bonding interactions, including those involving waters, are required to create functional metalloenzymes with high activity and turnover numbers comparable to those of native enzymes. While metalloproteins have been the major focus of metalloenzyme research for decades, metallo-DNAzymes, DNA molecules containing metal ions at the active site and displaying enzymatic activities, have emerged as a new class of metalloenzymes. We have been using in vitro selection to obtain from a large DNA library DNAzymes that are specific for metal ions and use spectroscopic methods to elucidate how and why DNAzymes can recognize metal ions selectively. We have also converted these DNAzymes into highly sensitive and selective sensors for metal ions, including those metal ions that are difficult to design using other methods, and demonstrated their applications in environmental monitoring, food safety, and medical diagnostics. The use of these metal-DNAzymes for imaging metal ions in living cells has also been established.



Tracy Handel 

University of California at San Diego  UCSD Skaggs School of Pharmacy & Pharmaceutical Sciences 

Host: Wei Liu

Catherine Murphy 

University of Illinois at Urbana-Champaign  Department of Chemistry 

Host: Dan Buttry


Chang-Guo Zhan 

University of Kentucky   

Host: Wei Liu


Greg Gillen 

National Institute of Standards and Technology (NIST)   

Host: Peter Williams

Jonathan Sweedler 

University of Illinois  Department of Chemistry 

Host: Jia Guo


Jeffrey Esko 

University of California at San Diego   

Host: Xu Wang

Thomas R Cech 

Eyring lecture 


Rebecca Schulman 

Johns Hopkins University   

Host: Hao Yan