B. S. 1986 Dongguk University, Seoul, Korea
M. S. 1988 Korea Advanced Institute of Science & Technology, Seoul, Korea
Ph. D. 2001 University of Illinois, Chicago
Postdoctoral Fellow 2001-2003 University of California, Berkeley
Postdoctoral Associate 2003-2004 Iowa State University

We focus on the development and application of the state-of-the-art techniques of solid-state nuclear magnetic resonance (SSNMR) spectroscopy to study diverse problems in biological science and modern materials related to future energy development. SSNMR spectroscopy covers a wide range of applications that cannot be addressed by liquid-state experiments and is a powerful tool to determine structural and dynamic information of sample systems of interest on the molecular level, regardless of their morphology.

Our recent research interests include:

• NMR crystallography: conformational and interfacial structures of protein-protein, protein-ligand, and protein-DNA complexes that are challenging to be co-crystallized into mesocrystals or microcrystals for X-ray diffraction but are practically feasible to be prepared into nanocrystals for SSNMR magic-angle spinning (MAS) experiments for structural and dynamic investigations.
• Characterizations of dynamic supramolecular structures of membrane-bound antimicrobial peptides and membrane proteins.
• Morphological characterization of polymeric membrane materials for fuel-cell applications or ionic separations.

1. "Pore Structure, Thinning Effect, and Lateral Diffusive Dynamics of Oriented Lipid Membranes Interacting with Antimicrobial Peptide Protegrin-1: ³¹P and ²H Solid-State NMR Study," S. Wi and C. Kim, J. Phys. Chem. B 112, 11402-11414 (2008).
2. "Chain structure of substituted stilbene–maleic anhydride alternating copolymer probed by solid-state NMR," M. Mao, C. Kim, S. Wi and S. R. Turner, Macromolecules 41, 387-389 (2008).
3. "Multiple-Quantum ¹³C Solid-State NMR Spectroscopy under Moderate Magic-Angle Spinning," S. Wi and S. J. Hwang, Chem. Phys. Lett. 426, 187-191 (2006).
4. "Long Range ¹H-¹⁹F Distance Measurement in Peptides by Solid-State NMR," S. Wi, N. Sinha and M. Hong, J. Am. Chem. Soc. 126, 12754-12755 (2004).
5. "Solid-State NMR Investigation of the Selective Perturbation of Lipid Bilayers by the Cyclic Antimicrobial Peptide RTD-1," J. J. Buffy, M. J. McCormick, S. Wi, A. Waring, R. I. Lehrer, and M. Hong, Biochemistry 43, 9800-9812 (2004).