Researching Life at the Molecular Level
Biophysicists seek to understand the fundamental processes of life by applying the methods of physics and chemistry to biological systems. Understanding these biological systems and their complex processes requires exquisitely detailed knowledge of molecular structures and molecular functions. To investigate life at this most basic level, biophysicists use some of the most powerful tools available-X ray crystallography, optical and laser spectroscopy, nuclear magnetic resonance (NMR) spectroscopy and advanced computational science.
Practical Applications of Biophysics
A relatively young and interdisciplinary field compared with the traditional sciences of physics and chemistry, biophysics holds great promise for new understandings and practical applications. One team of biophysicists at Cornell, the Structure-Based Drug Design Group, is applying advanced techniques for determining three-dimensional molecular structures to the development of new methods for creating novel drugs. Combining the X-ray diffraction patterns of crystals, the results of high-resolution, multidimensional NMR spectroscopy and advanced computational methods, the biophysicists study the molecular architecture of specific target proteins, such as viral components, at atomic resolution to gain insight into the design of new inhibitors that could bind and disable those proteins.
Collaborations among Diverse Faculty Members and Graduate Students
Biophysics at Cornell encompasses a diversity of research topics, as well as a number of collaborations involving shared ideas, facilities and materials. Research is often cooperative, usually interdisciplinary, and occasionally even somewhat freewheeling. A biophysicist trained in chemistry collaborates with a materials scientist to discover why the molecular structure of a spider's dragline silk makes it five times stronger than steel. Those researchers employ the same NMR and X-ray diffraction techniques used by the biochemists engaged in chemical prospecting to identify and isolate natural substances with potential medicinal value. Several researchers study cell membranes. One lab concentrates on the results that can be achieved with the technique of fast-chemical kinetics. Another group develops new optical techniques for imaging cells. Yet another examines proteins, phospholipids and cholesterol in biomembranes. Energy transfer among proteins during photosynthesis is another group's interest. And questions about signaling, or the flow of information between and among cells, figure in the work of several groups.
Excellent Career Opportunities
Because much of the current biophysics research at Cornell has great potential for solving long-standing problems in medicine, biomedical engineering and agriculture, graduates of Cornell's doctoral program in biophysics have a variety of career options. They teach, conduct research, work for such government agencies as the National Institutes of Health and the Department of Energy and pursue a range of opportunities in private industry-from small start-up companies and large, microelectronics-based corporations to investment and consulting firms. Among national science agencies, private foundations and large corporations, including pharmaceutical companies, there is great interest in biophysics.
Protein Structure and Function Is Key
One of the exciting challenges in biophysics is to understand the shape of protein molecules, how the molecules fold and how this folding affects their functions. The topic's importance is evident if you consider that enzymes, which are proteins, regulate every one of the 10,000 or so chemical reactions that take place in each living cell. Many protein molecules have already been described-isolated, purified, crystallized and mapped, with all of their hundreds of amino acids identified and pinpointed to an exact location. But protein molecules do not sit still. In their biologically active forms, they undergo librations and conformational transitions in response to their environment. A true picture of a protein must also include this dynamic character, a difficult topic of current investigation.