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Chemistry and Biology: Making the Connections
Summary: Catherine Drennan's research uses X-ray crystallography to study the structure and function of metalloproteins. Her HHMI project involves a freshman chemistry course that will excite undergraduates about chemistry and demonstrate the connection between chemistry and biological processes, a training program for postdoctoral fellows and graduate students in interdisciplinary teaching, an undergraduate biochemistry association at MIT, and an interdisciplinary summer undergraduate research program.
Project Summary
My goals as a biochemist and educator are to help students appreciate that chemical principles underlie all biological processes, to inspire students to take chemistry courses beyond the institutional requirements, and to train teaching assistants (TAs) in an interdisciplinary approach to education. The first component of my HHMI project is a freshman chemistry course that will provide a mechanism for getting students excited about chemistry early in their undergraduate careers. This interdisciplinary course will be taught in two parts: the first part will be taught by a physical chemist and will cover atomic theory, bonding, and thermodynamics; the second part will be taught by me, a biochemist, and will incorporate biological examples to cover acid-base equilibrium, oxidation-reduction reactions, transition metals, and kinetics. I plan to develop problem set questions that have biological relevance and touch on research conducted in the MIT chemistry department.
I will recruit graduate students and possibly postdoctoral fellows to be TAs. Because the TAs will do most of the problem set instruction, it is important that they feel comfortable with the biology examples and other interdisciplinary material covered in the course. A week-long summer boot camp for TAs will show them how chemical principles can be applied to multiple fields and help them incorporate biological examples into their teaching of chemistry. During the training we will delve into the specifics of how to present the freshman chemistry course material, what we want the students to take away, where students typically have problems, and how the TAs can help. We will also spend some time doing team-building exercises. The goal is that the TAs will become more comfortable with the material (including the biology examples), feel as though they are an important part of the freshman chemistry team, and be excited to be part of creating the course.
Another component of my HHMI project will be the development of the MIT Undergraduate Biochemistry Association (MUBA), a group that will help compensate for lack of a formal biochemistry program at MIT. Our target audience is any student interested in biological chemistry. Following the freshman chemistry course, the MUBA will provide chemistry students with a venue for continued dialog with non-chemistry majors and with academic advice and other mentoring support. In addition, MUBA will put together a guide for students whose interests lie at the interface of chemistry and biology to help them find appropriate laboratories to carry out undergraduate research. As an undergraduate chapter of the American Society for Biochemistry and Molecular Biology, the MUBA will also provide MIT students with a research connection on a national level.
A third project component will be the Summer Undergraduate Research Program in Chemical Biology, a 10-week program to encourage undergraduates with quantitative backgrounds to conduct research in biology laboratories and to encourage biology students to conduct research in chemistry or physics laboratories. In addition to the laboratory research, students will attend workshops on topics such as scientific ethics, biochemistry research at MIT and scientific speaking. The target audience will be MIT and non-MIT undergraduates, including those from groups underrepresented in the sciences.
Research Summary
My laboratory uses X-ray crystallography to study the structure and function of metalloproteins. Our research focuses on enzymes that contain complex metallocofactors and catalyze challenging chemical reactions, such as those that use organic radicals or form organometallic bonds. We are interested in providing detailed three-dimensional information about the nature of the complex metallocofactors and in understanding how the protein environment modulates the reactivity of these metal centers. Through biochemical and biophysical analysis, our long-term goal is to use crystallography to capture structures of proteins in various conformational states to investigate enzyme mechanisms and the role of conformational change in protein function.
Within the area of metalloprotein biochemistry, the systems that we study fall into three main categories: carbon fixation, radical reactions, and metal uptake. Many metalloproteins in these categories have historically eluded crystallographic characterization due to issues of oxygen sensitivity, conformational flexibility, heterogeneity, or structural complexity. My laboratory has specialized in tackling and solving these difficult crystallographic problems.
Last updated September 2006
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