Investigators in this focus area study the activity of proteins in the context of protein structure, and investigate interactions of proteins with natural ligands or ligands of modified or novel function. X-ray crystallography, NMR, EPR, visual spectroscopy, computational modeling, mass spectrometry, organic synthesis, and recombinant DNA techniques are among the broad range of methods used. Our faculty and up-to-date facilities provide a range of opportunities for our undergraduate and graduate students, and postdoctoral fellows to engage in interdisciplinary research in protein structure, function and design.
The Max T. Rogers NMR facility, located in the Chemistry building immediately adjacent to Biochemistry, contains 7 solution and 3 solid-state NMR spectrometers ranging from 300 to 600 MHz, with a state-of-the-art Varian Inova-600 serving as the primary instrument for biomolecular studies. In the summer of 2004, a 900 MHz spectrometer with both solution and solid-state capabilities and a cryogenically cooled triple-resonance probe will be installed on the MSU campus.
We are excited about a collaboration among structural biologists and life scientists from 7 institutions, including four principal members of the Michigan Life Science Corridor (Michigan State University, University of Michigan, Wayne State University, and the Van Andel Research Institute.) This consortium is building a state-of-the-art user facility for macromolecular crystallography at the Advanced Photon Source (APS) at Argonne National Laboratory. The synchrotron X-ray radiation from true beamlines is well suited for a wide range of crystallographic experiments.