Degrees Myriad Genetics (2005-2008) Ph.D. (2003), University of California, Riverside (Dallas Rabenstein) B.S. (1992), Oregon State University; Quanterra Environmental Services (1994-1997) Biography Dr. Spain directs the shared instrument facility within the chemistry department, which includes overseeing the day-to-day operation of the NMR, mass spectrometry, and optical facilities. This involves teaching new and ongoing students how to properly utilize the available instrumentation along with method development, maintenance, tuning, optimization, and calibration of the instrumentation. Further roles of the Director of Instrumentation include planning long term needs of the department for instrumentation acquisition and teaching courses in analytical chemistry. In addition, Dr. Spain develops and maintains the department's intranet site and shared instrument facility wiki site.

Dr. Spain's primary research interests involve using NMR and mass spectrometry to solve problems in the area of biological chemistry. NMR is a powerful analytical technique that can provide site specific binding information that other instrumentation cannot. Furthermore, NMR can be used to elucidate the exchange kinetics of a wide variety of interesting problems.

Shi, T.; Spain, S.M.; Rabenstein, D.L. A striking periodicity of the cis/trans isomerization of proline imide bonds in cyclic disulfide-bridged peptides. Angew. Chem. Int. Ed. 2006, 45, 1433.

Spain, S.M.; Rabenstein, D.L. Characterization of the selenotrisulfide formed by reaction of selenite with end-capped phytochelatin-2. Anal. Bioanal. Chem. 2004, 378, 1414.

Shi, T.; Spain, S.M.; Rabenstein, D.L. Unexpectedly fast cis/trans isomerization of Xaa-Pro peptide bonds in disulfide-constrained cyclic peptides. J. Am. Chem. Soc. 2004, 126, 790.

Spain, S.M.; Rabenstein, D.L. Characterization of the acid/base and redox chemistry of phytochelatin analogue peptides. Anal. Chem. 2003, 75, 3712.

Rabenstein, D.L.; Shi, T.S.; Spain, S.M. Intramolecular catalysis of the cis-trans isomerization of proline peptide bonds in cyclic disulfide-containing peptides. J. Am. Chem. Soc. 2000, 122, 2401.