The amino-acid sequence of a protein encodes its three-dimensional structure, and this structure manifests itself in biological function. Using techniques that range from synthetic chemistry to cell biology, the Raines group is illuminating in atomic detail both the chemical basis and the biological purpose for protein structure and protein function. The efforts of the Raines group are leading to insights into the relationship between amino-acid sequence and protein function (or dysfunction), as well as to the creation of novel molecules with desirable properties. For example, they have discovered an RNA-cleaving enzyme that is in a multi-site human clinical trial as an anti-cancer agent; revealed that unappreciated forces—the n-to-pi* interaction and C5 hydrogen bond—stabilize all proteins; created hyperstable and human-scale synthetic collagens; and developed processes to synthesize proteins, catalyze their folding, and facilitate their entry into human cells, and to convert crude biomass into useful fuels and chemicals.
The research projects in the Raines laboratory are designed to reveal how biological phenomena can be explained with the principles of chemistry. The hypotheses are far-reaching, and testing them requires the use of techniques and ideas from diverse disciplines. This broad/deep training is appropriate for scientists who want to perform innovative and meaningful research at the widening interface between chemistry and biology.
Alumni from the Raines laboratory have exciting careers as faculty members at distinguished research universities, medical schools, and colleges; and as research scientists at innovative start-up companies, leading corporations, and government laboratories.