Contact Information:
Department of Chemistry and Biochemistry
University of California, San Diego
Natural Science Building, Rm 3117
9500 Gilman Drive, MC 0307
La Jolla, CA 92093-0307 USA

TEL: (858) 822-4707
FAX: (858) 822-4821
email: shpark@chem.ucsd.edu

Education:
Ph. D. in Physical Pharmacy (2000)
Seoul National University, Korea

M.S. in Physical Pharmacy (1995)
Seoul National University, Korea

B.S. in Pharmacy (1993)
Seoul National University, Korea

Publications:

1. Lee, B.J., Lee, T.W., Park, S.H., Aiba, H., Kojima, C., and Kyogoku, Y. Nuclear magnetic resonance study of complexes between CRP and its 22 and 28 base pair operators. J. Biochem. 117, 239-243 (1995).

2. Park, S.H., Lee, T.W., and Lee, B.J. Conformational change of cyclic AMP receptor protein by the binding of cyclic nucleotide. Biochem. Mol. Biol. Int. 40, 93-100 (1996).

3. Park, S.H., Lee, T.W., Hwang, E.S., Lee, S.K., Shin, C.G., and Lee, B.J. Binding aspect of cyclic AMP receptor protein to symmetrically synthetic 22-, 28-, and 30-base-pair lac promoters. J. Kor. Mag. Reson. Soc. 1, 24-32 (1997).

4. Kim, Y.K., Park, S.H., Lee, J.H., Kwak, J.H., and Lee, B.J. The preliminary study on the structure of Cop protein by CD and NMR. J. Kor. Mag. Reson. Soc. 3, 100-108 (1999).

5. Park, S.H., Kim, Y.K., Kwak, J.H., and Lee, B.J. Spectroscopic studies on the structural stability of Cop protein. Seoul Univ. J. Pharm. Sci. 25, 9-16 (2000).

6. Yoon, M.K., Park, S.H., Won, H.S., Na, D.S., and Lee, B.J. Solution structure and membrane-binding property of the N-terminal tail domain of human annexin I. FEBS Lett. 484, 241-245 (2000).

7. Won, H.S., Yamazaki, T., Lee, T.W., Jee, J.G., Yoon, M.K., Park, S.H., Otomo, T., Aiba, H., Kyogoku, Y., and Lee, B.J. Letter to the editor: Backbone NMR assignments of a high molecular weight protein (47 kDa), cyclic AMP receptor protein (Apo-CRP). J. Biomol. NMR 16, 79-80 (2000).

8. Park, S.H., Kim, Y.K., Park, J.W., Lee, B., and Lee, B.J. Solution structure of the antimicrobial peptide gaegurin 4 by 1H and 15N nuclear magnetic resonance spectroscopy. Eur. J. Biochem. 267, 2695-2704 (2000).

9. Won, H.S., Yamazaki, T., Lee, T.W., Yoon, M.K., Park, S.H., Kyogoku, Y., and Lee, B.J. Structural understanding of the allosteric conformational change of cyclic AMP receptor protein by cAMP binding. Biochemistry 39, 13953-13962 (2000).

10. Hong, Y.H., Park, S.H., Lee, K., and Lee, B.J. (2001) Structural Characterization of growth-related translatioinally controlled tumor protein P23. J. Kor. Mag. Reson. Soc. 5, 46-55 (2001).

11. Lee, T.W., Won, H.S., Park, S.H., Kyogoku, Y., and Lee, B.J. Detection of the protein-protein interaction between cyclic AMP receptor protein and RNA polymerase, by 13C-carbonyl NMR. J. Biochem. 130, 57-61 (2001).

12. Park, S., Park, S.H., Ahn, H.C., Kim, S., Kim, S.S., Lee, B., and Lee, B.J.  Structural study of novel antimicrobial peptides, nigrocins, isolated from Rana nigromaculata. FEBS Lett. 507, 95-100 (2001).

13. Won, H.S., Lee, T.W., Park, S.H., and Lee, B.J. Stoichiometry and structural effect of the cyclic nucleotide binding to cyclic AMP receptor protein. J. Biol. Chem. 277, 11450-11455 (2002).

14. Won, H.S., Park, S.H., Kim, H.E., Hyun, B., Kim, M., Lee, B., and Lee, B.J. Effects of a tryptophanyl substitution on the structure and antimicrobial activity of C-terminally truncated gaegurin 4. Eur. J. Biochem. 269, 4367-4374 (2002).

15. Park, S.H., Kim, H.E., Kim, C.M., Yun, H.J., Choi, E.C., and Lee, B.J. Role of proline, cysteine and a disulphide bridge in the structure and activity of the anti-microbial peptide gaegurin 5. Biochem. J. 368, 171-182 (2002).

16. Son, W.S., Kim, J.S., Kim, H.E., Park, S.H., and Lee, B.J. Structural studies on the antimicrobial peptide Brevinin 1E by spectroscopic methods. Spectroscopy 17, 127-138 (2003).

17. Park, S.H., Mrse, A.A., Nevzorov, A.A., Mesleh, M.F., Oblatt-Montal, M., Montal, M., and Opella, S.J. Three-dimensional structure of the channel-forming trans-membrane domain of virus protein “u” (Vpu) from HIV-1. J. Mol. Biol. 333, 409-424 (2003).

18. De Angelis, A.A., Nevzorov, A.A., Park, S.H., Howell, S.C., Mrse, A.A., and Opella, S.J. High-resolution NMR spectroscopy of membrane proteins in aligned bicelles. J. Am. Chem. Soc. 126, 15340-15341 (2004).

19. Park, S.H. and Opella, S.J. Tilt angle of a trans-membrane helix is determined by hydrophobic mismatch. J. Mol. Biol. 350, 310-318 (2005).

20. De Angelis, A.A., Jones, D.H., Grant, C.V., Park, S.H., Mesleh, M.F., and Opella, S.J. NMR experiments on aligned samples of membrane proteins. Methods Enzymol. 394, 350-382 (2005).

21. Nevzorov, A.A., De Angelis, A.A., Park, S.H., and Opella, S.J. Uniaxial motional averaging of the chemical shift anisotropy of membrane proteins in bilayer environments. In NMR Spectroscopy of Biological Solids (Ramamoorthy, A., Ed.) CRC Press pp. 177-190 (2005).

22. Opella, S.J., Park, S.H., Lee, S., Jones, D., Nevzorov, A., Mesleh, M., Mrse, A., Marassi, F.M., Oblatt-Montal, M., Montal, M., Strebel, K., and Bour, S. Struture and Function of Vpu from HIV-1. in Viral Membrane Proteins: Structure, Function and Drug Design (Fischer, W., Ed.) Kluwer Academic Publishers pp. 147-163 (2005).

23. Park, S.H., Mrse, A.A., Nevzorov, A.A., De Angelis, A.A., and Opella, S.J. Rotational diffusion of membrane proteins in aligned phospholipid bilayers by solid-state NMR spectroscopy. J. Magn. Reson. 178, 162-165 (2006).

24. Park, S.H., Prytulla, S., De Angelis, A.A., Brown, J.M., Kiefer, H., and Opella, S.J. High-resolution NMR Spectroscopy of a GPCR in aligned bicelles. J. Am. Chem. Soc. 128, 7402-7403 (2006).

25. Park, S.H., De Angelis, A.A., Nevzorov, A.A., Wu, C.H., and Opella, S.J. Three-dimensional structure of the trans-membrane domain of Vpu from HIV-1 in aligned phospholipid bicelles. Biophys. J. 91, 3032-3042 (2006).

26. Nevzorov, A.A., Park, S.H., and Opella S.J. Three-dimensional experiment for solid-state NMR of aligned protein samples in high field magnets. J. Biomol. NMR 37, 113-116 (2007). *Nevzorov, A.A. and Park, S.H. contributed equally to this work.

27. Park, S.H., Son, W.S., Kim, Y.J., Kwon, A.R., and Lee, B.J. NMR spectroscopic assessment of the structure and dynamic properties of an amphibian antimicrobial peptide (gaegurin 4) bound to SDS micelles. J. Biochem. Mol. Biol. 40, 261-269 (2007).

28. Sinha N, Grant, C.V., Park, S.H., Brown, J.M., and Opella S.J. Triple resonance experiments for aligned sample solid-state NMR of 13C and 15N labeled proteins. J. Magn. Reson. 186, 51-64 (2007).

29. Kim, M.J., Park, S.H., Opella, S.J., Marsilje, T.H., Michellys, P.Y., Seidel, H.M., and Tian, S.S. NMR structural studies of interactions of a small, nonpeptidyl top mimic with the thrombopoietin receptor extracellular juxtamembrane and transmembrane domains. J. Biol. Chem. 282, 14253-14561 (2007).

30. Park, S.H. and Opella, S.J. Conformational changes induced by a single amino acid substitution in the trans-membrane domain of Vpu: Implication of HIV-1 susceptibility to channel blocking drugs. Protein Sci. Online published (2007).

31. Park, S.H. and Opella, S.J. Structure and dynamics of the membrane-bound form of Pf1 coat protein: Implications for the structural rearrangement that occurs during virus assembly. J. Mol. Biol. Submitted for publication (2007).