Characterization of Solvent-Macromolecule Interactions using Dissolution Dynamic Nuclear Polarization
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abstract
With this new award, the Chemical Structure, Dynamics and Mechanisms A Program (CSDM-A) of the Division of Chemistry supports Professor Christian B. Hilty of Texas A&M University in a project that will use magnetic resonance techniques to examine the structures of proteins in solution. These investigations will allow a determination of the way solvents such as water affect the shape and functions of the proteins they interact with. Since proteins play crucial roles in life processes and often carry out their functions in water solutions, these studies will impact research in molecular biology and the biomedical sciences. The investigator will also develop a series of web-based modules, aimed at middle school to high school students, which will highlight the importance of molecular structure in chemistry and biology.The proposed research will employ nuclear hyperpolarization based NMR techniques to investigate site specific and time dependent solvent-protein interactions. NMR spectra acquired after mixing the protein with hyperpolarized solvent will reveal polarization transferred to sites on the protein. The distribution of polarization on the protein will be used to derive solvent binding sites, contact areas and protein structure.
