Education：

State Univ. of New York at Stony Brook(USA)(Ph.D.) (2004)
National Tsing Hua University(M.S.) (1994)
National Taiwan Normal University(B.S.) (1992)

Journal Articles：

1. C. C. Chen, W. Hsu, K. C. Hwang, J. R. Hwu, C. C. Lin, and J. C. Horng*. Contributions of cation-π interactions to the collagen triple helix stability. Arch. Biochem. Biophys. 2011, 508, 46-53. (DOI:10.1016/j.abb.2011.01.009)
    
2. C. C. Chen, W. Hsu, T. C. Kao, and J. C. Horng*. Self-assembly of short collagen-related peptides into fibrils via cation-π interactions. Biochemistry 2011, 50, 2381-2383. link
    
3. Y. S. Chen, C. C. Chen, and J. C. Horng*. Thermodynamic and kinetic consequences of substituting glycine at different positions in a Pro-Hyp-Gly repeat collagen model peptide.Biopolymers (Pept. Sci.) 2011, 96, 60-68. link
    
4. T. Y. Zheng, Y. J. Lin, and J. C. Horng*. Thermodynamic consequences of incorporating 4-substituted proline derivatives into a small helical protein. Biochemistry 2010, 49, 4255-4263. link
    
5. Y. C. Chiang, Y. J. Lin, and J. C. Horng*. Stereoelectronic effects on the transition barrier of polyproline conformational interconversion. Protein Sci. 2009, 18, 1967-1977. (DOI: 10.1002/pro.208)
    
6. J. H. Cho, S. Sato, J. C. Horng, B. Anil, and D. P. Raleigh. Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability. Arch. Biochem. Biophys. 2008, 469, 20-28.
    
7. J. C. Horng, F. W. Kotch, and R. T. Raines. Is glycine a surrogate for a D-amino acid in the collagen triple helix? Protein Sci. 2007, 16, 208-215.
    
8. J. C. Horng, A. J. Hawk, Q. Zhao, E. S. Benedict, S. D. Burke, and R. T. Raines. A macrocyclic scaffold for the collagen triple helix. Org. Lett. 2006, 8, 4735-4738.
    
9. Y. Li, J. C. Horng and D. P. Raleigh. pH Dependent thermodynamic and amide exchange studies of the C-terminal domain of the ribosomal protein L9: implications for unfolded state structure.Biochemistry 2006, 45, 8499-8506.
    
10. J. C. Horng and R. T. Raines. Stereoelectronic effects on polyproline conformation. Protein Sci.2006, 15, 74-83.
     
11. K. L. Maxwell, D. Wildes, A. Zarrine-Afsar, M. A. de los Rios, A. G. Brown, C. T. Friel, L. Hedberg, J. C. Horng et al. Protein folding: Defining a ""standard"" set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci. 2005, 14, 602-616.
     
12. J. C. Horng, J. H. Cho, and D. P. Raleigh. Analysis of the pH-dependent folding and stability of histidine point mutants allows characterization of the denatured state and transition state for protein folding. J. Mol. Biol. 2005, 345, 163-173.
     
13. J. C. Horng, S. M. Tracz, K. J. Lumb, and D. P. Raleigh. Slow folding of a three-helix protein via a compact intermediate. Biochemistry 2005, 44, 627-634.
     
14. J. C. Horng, S. J. Demarest, and D. P. Raleigh. pH dependent stability of the human α-lactalbumin molten globule state: contrasting roles of the 6 to 120 disulfide and the β-subdomain at low and neutral pH. Proteins 2003, 52, 193-202.
     
15. J. C. Horng and D. P. Raleigh. Φ-Values beyond the ribosomally encoded amino acids: kinetic and thermodynamic consequences of incorporating trifluoromethyl amino acids in a globular protein. J. Am. Chem. Soc. 2003, 125, 9286-9287.
     
16. Y. Wei, J. C. Horng, A. C. Vendel, D. P. Raleigh, and K. J. Lumb. Contribution to stability and folding of a buried polar residue at the CARM1 methylation site of the KIX domain of CBP.Biochemistry 2003, 42, 7044-7049.
     
17. J. C. Horng, V. Moroz, and D. P. Raleigh. Rapid cooperative two-state folding of a miniature a-b protein and design of a thermostable variant. J. Mol. Biol. 2003, 326, 1261-1270.
     
18. J. C. Horng, V. Moroz, D. J. Rigotti, R. Fairman, and D. P. Raleigh. Characterization of large peptide fragments derived from the N-terminal domain of the ribosomal protein L9: definition of the minimum folding motif and characterization of local electrostatic interactions. Biochemistry2002, 41, 13360-13369.
     
19. S. J. Demarest, J. C. Horng, and D. P. Raleigh. A protein dissection study demonstrates that two specific hydrophobic clusters play a key role in stabilizing the core structure of the molten globule state of human α-lactalbumin. Proteins 2001, 42, 237-242.