MRI: Acquisition of a Circular Dichroism Spectrometer for Research and Training of Undergraduate Students

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With this award from the Major Research Instrumentation (MRI), the Chemistry Research Instrumentation and Facilities (CRIF) as well as the Chemistry of Life Processes (CLP) programs, Professor Kumar Sinniah from Calvin College and colleagues David Benson, Douglas Vander Griend, Rachael Baker and Jiyan Ma have acquired a circular dichroism (CD) spectrometer. Many chemical and biological molecules are chiral (having structures that are not superimposable - like our hands). Chiral molecules that are prevalent in living organisms can exist in two forms. These can be described as having left-handed or right-handed conformations. A CD spectrometer can determine which form or whether a mixture of both is present. The spectrometer can follow changes as the chiral molecule binds to another molecule (ligand), rearranges its structure, or reacts (perhaps with a drug or an antibody). Therefore, CD spectroscopy is ideally suitable for probing protein (or other macromolecular) structures or changes to structures due to environmental conditions or to the binding of a ligand. CD spectroscopy has been widely used for three types of measurements: identifying the structure of proteins, studying the conformational changes during folding and unfolding of proteins, and determining the energetics involved in binding interactions and protein unfolding. This spectrometer is used by undergraduates. While being trained to use this important tool, the research experience prepares the students for future careers and advanced degrees in medical and scientific fields. This award is aimed at enhancing education and training of undergraduates and advancing research, especially in areas such as: (a) investigating the binding interaction between G-quadruplex DNA and insulin, (b) measuring the far ultra-violet and the near-infrared circular dichroism to understand the contribution of cysteine-tyrosine post-translational modifications on protein stability and function, (c) investigating the folding and unfolding thermodynamics of proteins and peptide systems, (d) investigating the functional role of Ras monoubiquitination, and (e) monitoring the folding, stability, and conformational conversion of various prion protein mutants.