From the Chair
Welcome from the faculty, staff, and chemistry majors of the classes of 2010 and 2011 to the 24 new chemistry majors in the class of 2012! Please feel free to join us for our weekly seminars, Journal Club meetings, Periodic Table, and the spring picnic in May. You will now receive the “Weekly Beaker” in your email box informing you of these events, career and summer opportunities, and more. We look forward to the “quality time” we will spend with you next year in Advanced Lab, Quantum and Thermo.
The new majors are:
|Ahmed, Sameena N.||Modlin, Chelsea E.|
|Benson, Katherine A.||Morrissey, James L.|
|Cammarota, Ryan C.||Olson, Erik D.|
|Deeg, Kathryn S.||Patel, Puja H.|
|Demke, Owen N.||Raberg, Jonathan H.|
|Dunn, Peter L.||Roberts, Sean F.|
|Finke, Cody E.||Robinson, Karen E.|
|France, Katherine A.||Skoglund, Mark R.|
|Kemper, Anthony T.||Smyth, Alison M.|
|Kempers, Brian T.||Snow, Kaj K.|
|Kittaka, Rachel S.||Walters, Diane M.|
|Lau, Chelsea E.||Yeung, Alfred|
Friday, April 16, 2010
The Scripps Research Institute
Activity-based proteomics - Applications for enzyme and inhibitor discovery
Genome sequencing projects have revealed that eukaryotic and prokaryotic organisms universally possess a huge number of uncharacterized enzymes. The functional annotation of enzymatic pathways thus represents a grand challenge for researchers in the post-genomic era. To address this problem, we have introduced chemical proteomic and metabolomic technologies that globally profile enzyme activities in complex biological systems. These methods include activity-based protein profiling (ABPP), which utilizes active site-directed chemical probes to determine the functional state of large numbers of enzymes in native proteomes. In this lecture, I will describe the integrated application of ABPP and complementary metabolomic methods to discover and functionally annotate enzyme activities in mammalian (patho)physiological processes, including neurotransmitter metabolism and cancer malignancy. I will also present competitive ABPP platforms for developing selective inhibitors of enzymes and discuss ongoing challenges that face researchers interested in assigning protein function using chemoproteomic methods.
Journal Club Meets This Week
Journal Club meets this Thursday at noon in Mudd 171 to discuss a paper relating to this week’s seminar. Go to the following for information about what to read beforehand: http://apps.carleton.edu/curricular/chem/events/?category=171005&no_search=1.
Lunch With Comps Visitors
As the spring comps season is now heating up, I want to let you all know that there will be opportunities for majors to go for lunch with comps visitors over the next few weeks. There is typically a lunch in their schedule with students who are NOT in the comps group they’re here to work with. Attending these lunches is a fantastic way to learn more about the visitors’ institutions, their science, and their perspective on the discipline. This will make you a better chemist, as you will have examples of multiple perspectives on important issues! At the same time, it will help the visitors to get a feeling for Carleton and the students (you!).
The first such lunch is with Prof. Benjamin Cravatt from The Scripps Research Institute. Lunch will be Friday at noon. Meet in the Mudd hallway, and if you’re off board, the department will pay for your lunch.
Have a great lunch!
Chemistry Group Comps Presentation
Monday, April 19, 2010
Chris Clark, Henry Heitzer, Lindsey Madison, Colin Russell and Laura Sofen
Molecular Catch and Release: Metal-Ligand Coordination Chemistry
Professor Ken Raymond is a bioinorganic chemist at the University of California at Berkeley. His seminal work focused on siderophores, iron-chelating complexes prevalent in biological systems. This led him to investigate chelating agents designed specifically to sequester plutonium as a way of removing it from the body. His work with chelating agents has recently extended to supramolecular metal-ligand complexes. These structures self-assemble from relatively simple components into molecular reaction vessels that act as “nanozymes”, catalyzing reactions involving small and medium-sized cations. Thermodynamics, kinetics, and the structural components of supramolecular structures have been investigated on a variety of catalyst reactions and with an array of NMR techniques.