个人简介
B.S. Illinois Institute of Technology, 1969
Ph.D. University of Minnesota, 1973
研究领域
Biophysical chemistry/magnetic resonance spectroscopy of complex biological structures
Biophysical Chemistry; Magnetic Resonance Spectroscopy of Complex Biological Structures
There are currently two fundamental directions to our research. In one of these, biological membranes and complex biomolecules are being studied using nuclear magnetic resonance (NMR) and electron spin resonance (ESR) techniques. Current areas of interest include two ion transporting enzymes (kidney Na,K-ATPase and muscle Ca-ATPase), and two membrane-associated signalling enzymes (protein kinase C and phospholipase C. The ATPases use the free energy of hydrolysis of ATP to transport sodium, potassium or calcium across cell membranes against large concentration gradients. Protein kinase C is an intracellular mediator of hormonal and neurotransmitter stimuli and is also the receptor for phorbol ester tumor promoters. The geometry and active site structures of these complex systems are being examined by several methods. In one, we employ paramagnetic probes, such as Mn and Gd ions, Cr-nucleotide complexes and spin label analogues of enzyme substrates and inhibitors. Such probes perturb the nuclei in their vicinity and alter the nuclear relaxation rates. Quantitation of such effects can provide distances between the probes and nuclei on the enzyme surface. Another method, transferred nuclear Overhauser enhancement, permits additional studies of the conformation of substrates and activators at the active sites of these enzymes.
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Structural consequences of divalent metal binding by the adenylyl cyclase toxin of Bordetella pertussis. Rhodes CR, Gray MC, Watson JM, Muratore TL, Kim SB, Hewlett EL, Grisham CM. Arch Biochem Biophys. 395, 169-76 (2001).
Influence of lipid on the structure and phosphorylation of protein kinase C alpha substrate peptides. Vinton BB, Wertz SL, Jacob J, Steere J, Grisham CM, Cafiso DS, Sando JJ. Biochem J. 330, 1433-42 (1998).
Intermolecular chiral recognition probed by enantiodifferential excited-state quenching kinetics. Stockman TG, Klevickis CA, Grisham CM, Richardson FS. J Mol Recognit. 9, 595-606 (1996).
31P NMR investigation of energy metabolism in perifused MMQ cells. Goger MJ, Login IS, Fernandez EJ, Grisham CM. Magn Reson Med. 3, 584-91 (1994).