Through TSRI Educational Outreach Programs, Teachers, and High School Students may contribute to research ongoing in the Romesberg lab.

For the Summer of 2008, we are most interested in hosting a student/teacher team to learn how carbon-deuterium bonds may be used to probe dynamics and electrostatics in proteins.

Summer project abstract: Understanding how proteins fold and function is central goal of both the physical biochemistry and biology.   The most fundamental approach to understanding the detailed structure and activity of any molecule, including proteins, is based on an understanding of its constituent bonds.   The most direct method to characterize chemical bonds is to characterize their infrared absorption.   For example, stronger bonds absorb at higher frequencies than weaker bonds, and bonds in highly fluctuating environments have broader absorptions than those in structurally rigid environments.   While infrared spectroscopy has provided detailed information about the chemical bonds in small molecules, proteins are difficult to characterize using this approach, because they have so many bonds with overlapping absorptions that none may be specifically resolved.   To circumvent this problem, we use synthetic chemistry to construct proteins with specific carbon-hydrogen bonds selectively replaced with carbon-deuterium bonds.   This isotopic substitution shifts the absorption of bond to a region of the protein's infrared spectrum that does not naturally contain protein bond absorptions, but does not otherwise perturb the protein.   This isotopic shift allows bond-specific characterization of different parts of any protein using methods such as laser spectroscopy and Fourier-transform infrared spectroscopy.   Efforts in the lab currently focus on the protein cytochrome c which has served as a paradigm for protein folding and biological electron transfer.   A summer research internship contributing to these efforts could involve any aspect of the project, including for example, chemical protein synthesis, protein sample preparation and handling, steady-state or time-resolved spectroscopy, and data analysis.