Master of Science in Chemistry and Chemical Biology - Biophysical

The M.S. program consists of 30 credit hours of coursework. In favorable circumstances, it is possible that the program might be completed over a single academic year though most applicants require more time in the program. As the academic backgrounds and personal/professional goals of each student will differ, we anticipate significant diversity in the programs of study in the M.S. degree and therefore do not prescribe a rigid set of courses as prerequisites or requirements though we would ordinarily anticipate that the majority of the credits are taken in chemistry and related subjects at suitably high levels. Your program of study will be adapted to your individual interests and needs in consultation with the M.S. Graduate Program Director, and will likely include coursework selected from across Cornell?s campus.

The M.S. program is designed for those who wish to obtain further education in the field of chemical sciences broadly understood, and to develop their ability for critical inquiry, independent research, and teaching. Research-degree students are expected to give evidence of mature purpose by initiating and pursuing their own programs, as such the award of the MS degree is contingent upon the completion of a master?s research project documented through the preparation of an archive document presented to the student?s special committee and to the Graduate School. In the fall of the first year, it is expected that each student will be enrolled in Chem 5110, which provides an introduction to the vast world of tools and opportunities for chemical research, found in both our department and across the campus.

Biophysical chemistry studies the properties of biological molecules along with the principles and methods of physics and physical chemistry. Experimentation and computation combine at Cornell to probe the structure, dynamics, interactions and functions of individual biological macromolecules and supramolecular complexes. Primary biological conformational processes such as protein folding, protein dynamics and binding are addressed by theoretical methods and experiments. X-ray crystallography determines structures of biologically active molecules such as anti-tumor agents, immunosuppressants and protein complexes. Fluorescence spectroscopy, microscopy, and flow cytometry measure ligand binding and the structural interactions of cell surface receptors and lipids critical for signal transduction during immune responses and carcinogenesis. Laser photolysis techniques are used to study electron transfer reactions and release photolabile ligands for triggering receptors in nerve cells. Electron spin resonance (ESR) spectroscopy allows investigation of the dynamics of membranes and protein-lipid interactions.

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