Ding-Kwo Chang

Molecular Biophysics

Ding-Kwo Chang (張定國)

    886-2-27898594
    886-2-27831237
    dkgatechem
Research Fellow(1997-);B.S., National Taiwan University (1973);Ph.D., University of Wisconsin- Madison, USA(1984);Postdoctoral Fellow, University of California- San Diego(1984-85);Postdoctoral Fellow, University of Alberta(1985-87);Instructor, University of Alabama Birmingham (1987 - 90);Research Fellow, Keck Center for Computational Biology, Rice University(1991); Associate Research Fellow(1991-1997);
Research Interests

Conformation of HIV-1 envelope glycoprotein fragments and its folding kinetics to understand binding between CD4, coreceptors and HIV-1 envelope glycoprotein.
Protein-membrane interactions and proteomics from bioinformatics.
Search of SARS coronavirus cellular receptor and inhibitors of viral attachment to the target cell. Development of antibody to the SARS virus for diagnosis and SARS treatment.
Development of inhibitors of HIV-1, SARS coronavirus and other virus replication with derivatives of viral envelope fusion proteins.





Selected Publications
  1. Lin, S.-H.; Chang, D. K.; Chou, M.-J.; Huang, K.-J.; Shiuan, D. Peptide inhibitors of human HMG-CoA reductase as potential hypocholesterolemia agents. Biochim Biophy Res Comm 2015, 456, 104.
  2. Lin, Y.-J.; Wu, C.-Y.; Li, T. ; Hsiao, P.-W.; Chang, D. K. A Rapid and Sensitive Early Diagnosis of Influenza Virus Subtype via SERS. J Biosens Bioelectron 2014, 5, 2.
  3. Cheng, S.-F.; Sung, T.-C.; Chang, C.-C.; Chou, M.-J.; Chiang, Y.-W.; Chang, D. K. Kinetics Study on the HIV ‑ 1 Ectodomain Protein Quaternary Structure Formation Reveals Coupling of Chain Folding and Self-Assembly in the Refolding Cascade. J. Phys. Chem. B 2014, 118, 12827.
  4. Lin, K. C.; Chen, C. Y.; Chang, C. W.; Huang, K. J.; Lin, S. P.; Lin, S. H.; Chang, D. K.; Lin, M. R.; Shiuan, D. A Dodecapeptide (YQVTQSKVMSHR) Exhibits Antibacterial Effect and Induces Cell Aggregation Escherichia Coli. Appl Microbiol Biotechnol 2012, 94, 755.
  5. Wei, H. J.; Chang, W.; Lin, S. C.; Liu, W. C.; Chang, D. K.; Chong, P.; Wu, S. C. Fabrication of Influenza Virus-like Particles Using M2 Fusion Proteins for Imaging Single Viruses and Designing Vaccines. Vaccine 2011, 29, 7163.
  6. Chang, C. C.; Cheng, S. F.; Lin, C. H.; Chen, S. S. L.; Chang, D. K. Stability of gp41 Hairpin and Helix Bundle Assembly Probed by Combined Stacking and Circular Dichroic Approaches. Journal of Structural Biology 2011, 175, 406.
  7. Lin, C. H.; Lin, C. H. Chang, C. C., Cheng, S. F., Chang, D. K. An Efficient Production and Characterization of HIV-1 gp41 Ectodomain With Fusion Peptide in Escherichia Coli System. J. Biotech. 2011, 153, 48..
  8. Pan, Y. S.; Wei, H. J.; Chang, C. C.; Lin, C. H.; Wei, T. S.; Varecˇkov, E.; Wu, S. C.; Chang, D. K. Construction and Characterization of Insect Cell Derived Influenza VLP: Cell Binding and Fusion. J Biomed Biotech 2010 Article ID 506363.
  9. Cheng, S. F.; Chien, M. P.; Lin, C. H.; Chang, C. C.; Lin, C. H.; Liu, Y. T.; Chang, D. K. The Fusion Peptide Domain is the Primary Membrane-Inserted Region and Enhances Membrane Interaction of the Ectodomain of HIV-1 gp41. Mol Membe Biol 2010 27, 32.
  10. Chen, S. S. L.; Yang, P.; Ke, P.-Y.; Li, H.-F.; Chan, W.-E.; Chang, D. K.; Chuang, C.-K.; Tsai, Y.; Huang, S.-C. Identification of the LWYIK Motif Located in the Human Immunodeficiency Virus Type 1 Transmembrane gp41 Protein as a Distinct Determinant for Viral Infection. J. Virol. 2009, 83, 870.
  11. Chien, M. P.; Lin, C. H.; Chang, D. K. Recruitment of HIV-1 Envelope Occurs Subsequent to Lipid Mixing: A Fluorescence Microscopic Evidence. Retrovirology 2009, 6, 20.
  12. Lin, C. H.; Chang, C. C.; Cheng, S. F.; Chang, D. K. The Application of Perfluorooctanoate to Investigate Trimerization of the Human Immunodeficiency Virus-1 gp41 Ectodomain by Electrophoresis. Electrophoresis 2008, 29, 3175.
  13. Kantchev, E. A. B.; Chang, C. C.; Cheng, S. F.; Roche, A. C.; Chang, D. K. Direct solid-phase synthesis and fluorescence labeling of large, monodisperse mannosylated dendrons in a peptide synthesizer. Org Biomol Chem.2008, 6, 1377.
  14. Chang, D. K.; Cheng, S. F.; Kantchev, E. A.; Lin, C. H.; Liu, Y. T. Membrane interaction and structure of the transmembrane domain of influenza hemagglutinin and its fusion peptide complex. BMC Biol. 2008, 6, 2.
  15. Chien, M. P.; Jiang, S.; Chang, D. K. The function of coreceptor as a basis for the kinetic dissection of HIV type 1 envelope protein-mediated cell fusion. FASEB J. 2008, 22, 1179.
  16. Chang, D. K.; Hsu, C. S. Biophysical evidence of two docking sites of the carboxyl heptad repeat region within the amino heptad repeat region of gp41 of human immunodeficiency virus type 1. Antiviral Res. 2007, 74, 51.
  17. Chang, D. K.; Cheng, S. F. pH-dependence of intermediate steps of membrane fusion induced by the influenza fusion peptide. Biochem. J. 2006, 396, 557.
  18. Kantchev, E. A. B.; Chang, C. C.; Chang, D. K. Direct Fmoc/tert-Bu solid phase synthesis of octamannosyl polylysine dendrimer-peptide conjugates. Biopolymers 2006, 84, 232.
  19. Chang, D. K.; Cheng, S. F.; Lin, C. H.; Kantchev, E. A. B.; Wu, C. W. Self-association of glutamic acid-rich fusion peptide analogs of influenza hemagglutinin in the membrane-mimic environments: Effects of positional difference of glutamic acids on side chain ionization constant and intra- and inter-peptide interactions deduced from NMR and gel electrophoresis measurements. BBA. Acta-Biomembranes. 2005, 1712, 37.
  20. Kantchev, E. A. B.; Cheng, S. F.; Wu, C. W.; Huang, H. J.; Chang, D. K. Secondary structure, phospholipid membrane interactions, and fusion activity of two glutamate-rich analogs of influenzahemagglutinin fusion peptide. Arch. Biochem. Biophys. 2004, 425, 173.
  21. Cheng, S. F.; Wu, C. W.; Kantchev, E. A. B.; Chang, D. K. Structure and membrane interaction of the internal fusion peptide of avian sarcoma leukosis virus. Eur. J. Biochem. 2004, 271, 4725.
  22. Trivedi , V. D.; Cheng, S. F.; Wu, C. W.; Radhakrishnan Karthikeyan, R.; Chen, C. J.; Chang, D. K. The LLSGIV stretch of the N-terminal region of HIV-1 gp41 is critical for binding to a model peptide, T20. Prot. Engineering, 2003, 16, 311.
  23. Cheng, S. F.; Kantchev, A. B.; Chang, D. K. Fluorescence evidence for a loose self-assembly of the fusion peptide of influenza virus HA2 in the lipid bilayer.Mol. Memb. Biol. 2003, 20, 345.
  24. Wu, C. W.; Cheng, S. F.; Huang, W. N.; Trivedi, V. D.; Veeramuthu, B.; Kantchev, A. B.; Wu, W. G.; Chang, D. K. Effects of alterations of the amino-terminal glycine of influenza hemagglutinin fusion peptide on its structure, organization and membrane interactions. Biochim. Biophy. Acta 2003, 1612, 41.
  25. Hsu, C. H.; Wu, S. H.; Chang, D. K.; Chen, C. P. Structural characterizations of fusion peptide analogs of influenza virus hemagglutinin. J. Biol. Chem. 2002, 277, 22725.
  26. Chang, D. K.; Cheng, S. F.; Trivedi, V. D. Conformation and interaction with the membrane models of the amino-terminal peptide of influenza virus hemagglutinin HA2 at fusion pH.Arch. Biochem. Biophys. 2001, 396, 89.
  27. Chang, D. K.; Trivedi, V. D.; Cheng, S. F.; Francis, S. The leucine zipper motif of the envelope glycoprotein ectodomain of human immunodeficiency virus type 1 contains conformationally flexible regions as revealed by NMR and circular dichroism studies in different media. J. Pept. Res. 2001, 57, 234.
  28. Trivedi, V. D.; Yu, C.; Veeramuthu, B.; Francis, S.; Chang, D. K. Fusion induced aggregation of model vesicles studied by dynamic and static light scattering. Chem. Phys. Lipids 2000, 107, 99.
  29. Chang, D. K.; Cheng, S. F.; Trivedi, V. D.; Yang, S. H. The amino-terminal region of the fusion peptide of the influenza hemagglutinin HA2 inserts into the membrane with residues 16-18 at the aqueous boundary at acidic pH: implications on the conformational flexibility and oligomerization. J. Biol. Chem. 2000, 275, 19150.
  30. Chang, D. K.; Cheng, S. F.; Yang, S. H. A helix initiation motif, XLLRA, is stabilized by hydrogen bond, hydrophobic and van der Waals interactions. Biochim. Biophys. Acta. 2000, 1478, 39.
  31. Samuel, D.; Kumar, T. K. S.; Ganesh, D.; Jayaraman, G.; Yang, P. -W.; Chang, M. -M.; Trivedi, V. D.; Wang, S. -L.; Hwang, K. -C.; Chang, D. K.; Yu, C. Proline inhibits aggregation during protein refolding. Protein Sci. 2000, 9, 344.
  32. Chang, D. K.; Cheng, S. F.; Trivedi, V. D. Biophysical characterization of the structure of the amino-terminal region of gp41 of HIV-1: implications on viral fusion mechanis. J. Biol. Chem. 1999, 274, 5299.
  33. Chang, D. K.; Cheng, S. F.; Trivedi, V. D.; Lin, K. L. Proline affects oligomerization of coiled coil by inducing a kink in a long helix. J. Struc. Biol. 1999, 128, 270.
  34. Cheng, S. F.; Chang, D. K. Proline-induced kink in a helix arises primarily from dihedral angle energy: a molecular dynamics simulation on alamethicin. Chem. Phys. Lett. 1999, 301, 453.
  35. Chang, D. K.; Cheng, S. F.; Trivedi, V. D. Biophysical characterization of the structure of the amino-terminal region of gp41 of HIV-1: implications on viral fusion mechanism. J. Biol. Chem. 1999, 274, 5299.
  36. Chang, D. K.; Cheng, S. F. Determination of the equilibrium micelle-inserting position of the fusion peptide of gp41 of human immunodeficiency virus type 1 at amino acid resolution by exchange broadening of amide proton resonances. J. Biomol. NMR, 1998 Nov., 12, 549.
  37. Chien, W. J.; Cheng, S. F.; Chang, D. K. Determination of binding constant of a protein kinase C substrate, NG(28-43), to sodium sodecyl sulfate via diffusion coefficient measured by pulsed field gradient NMR. Anal. Biochem. 1998, 264, 211.
  38. Sivaraman, T.; Kumar, T. K. S.; Chang, D. K.; Lin, W. Y.; Yu, C. Events in the kinetic folding pathway of a small, all b-sheet protein. J. Biol. Chem.1998, 273, 10181.
  39. Chang, D. K.; Cheng, S. F.; Chien, W. J. The amino-terminal fusion domain peptide of HIV-1 gp41 inserts into the sodium dodecyl sulfate micelle primarily as a helix with a conserved glycine at the micelle-water interface. J. Virology, 1997, 71, 6593.
  40. Chang, D. K.; Chien, W. J.; Cheng, S. F. The FLG motif in the N-terminal region of gp41 of HIV-1 adopts a type I b-turn in aqueous solution and serves as the initiation site for helix formation. Eur. J. Biochem., 1997, 247, 896.
  41. Chang, D. K.; Chien, W. J.; Cheng, S. F.; Chen, S. T. NMR and circular dichroism studies on the conformation of a 44-mer peptide from a CD4-binding domain of human immunodeficiency virus envelope glycoprotein. J. Peptide Res. 1997, 49, 432.
  42. Chang, D. K.; Chien, W. J.; Arunkumar, A. I. Conformation of a protein kinase C substrate NG(28-43), and its analog in aqueous and sodium dodecyl sulfate micelle solutions. Biophysical J. 1997, 72, 554.
  43. Yang, Y.; Huang, L.; Pon, R. T.; Cheng, S. F.; Chang, D. K.; Lown, J. W. Solution structure studies of the cobalt complex of a bleomycin functional model bound to d(CGCAATTGCG)2 by two-dimensional nuclear magnetic resonance methods and restrained molecular dynamics simulation. Bioconjugate Chemistry 1996, 7, 670.
  44. Chang. D. K.; Cheng, S. F. On the importance of van der Waals interaction in the groove binding of DNA with ligands: restrained molecular dynamics study. Int. J. Biol. Macromol. 1996, 19, 279.
  45. Chang, D. K.; Cheng, S. F. Circular dichroic study on the secondary structural change induced by complex formation of a peptide derived from a CD4 binding site of HIV-1 envelope glycoprotein gp120 and a peptide from N-terminal domain of CD4. Lett. Pept. Sci. 1996, 3, 293.
  46. Chien, W. J.; Lin, S. C.; Chang, D. K. Self-diffusion measurement on synthetic biopolymers via pulsed field gradient NMR spectroscopy. Bull. Inst. Chem., Acad. Sinica 1996, 43, 53.
  47. Jayaraman, G.; Kumar, T. K.; Sivaraman, T.; Lin, W. Y.; Chang, D. K.; Yu, C. Thermal denaturation of an all b-sheet protein-identification of a stable partially structured intermediate at high temperature. Int. J. Biol. Macromol. 1996, 18, 303.
  48. Chang, D. K.; Chien, W. J.; Cheng, S. F. Characterization of conformation and dynamics of CD4 fragment (81-92) TYICEVEDQKEE and its benzylated derivative by 1H NMR spectroscopy and molecular modeling: relevance of conformation to biological function. J. AIDS Hum. Retrov. 1996, 11, 223.
  49. Chang, D. K.; Cheng, S. F.; Chien, T. L. Molecular mechanics calculation on the complexes between analogues of Hoechst 33258 and d(CGCGAATTCGCG)2: influence of bulky group substitution on base pair preference of DNA mi?nor groove binders. Can. J. Chem. 1995, 73, 878.
  50. Chang, D. K.; Liang, C. C. Influence of bulky side chains of amino acids on the solution conformation of peptide fragment (81-92) derivatives of CD4, TYICEVEDQKEE, as studied by NMR spectroscopy and molecular modeling. Biochimca et Biophsica Acta 1994, 1205, 262.
  51. Chang, D. K.; Chien, W. J. Application of multi-dimensional NMR technique to the structure-activity relationship of biopolymers. Instruments Today 1994, 15, 47.
  52. Bhaskaran, R.; Huang, C.-C.; Tsai, Y.-C.; Jayaraman, G.; Chang, D.-K.; Yu, C. Cardiotoxin II from Taiwan cobra venom, Naja naja atra. J. Biol. Chem. 1994, 269, 23500.
  53. Bhaskaran, R.; Huang, C.-C.; Chang, D.-K.; Yu, C. Cardiotoxin III from the Taiwan cobra (Naja naja atra) determination of structure in solution and comparison with short neurotoxins. J. Mol. Biol. 1994, 235, 1291.
    B.Conference
  1. Michnicka, M.; Chang, D. K.; King, G. C. NMR Studies of 13C- and 15N-labelled RNA Species. Faseb J. 1992, A32, 177.
  2. King, G. C.; Chang, D. K.; Harper, J. W.; Logsdo, N.; Michnicka, M. Solution Structure of an HIV-1 Tar RNA Fragment and Its Interaction with Tat-derived Peptides. Faseb J. 1992, A150, 861.
  3. King, G. C.; Xi, Z.; Chang, D. K.; Michnicka, J. M.; Khabashesku, O.; Harper, J. W. Isotope-lablled RNAs from HIV-1. J. Cell. Biochem. 1993, S17C, 242.
  4. Chang. D. K.; Liang, C. C. Study of Solution Conformation of CD4 Peptide and Its Benzylated Derivatives by Two Dimensional 1H NMR Spectroscopy. 34th Experimental NMR Conference, St. Louis, MO, U.S. 1993.
  5. Chang, D. K.; Liang, C. C. Three Dimensional Structure Determination of HIV-1 Glycoprotein Fragment (418-461) by Proton NMR Spectroscopy and Molecular Modeling. 10th FAOB Symposium on Protein Research 1993, SS-76.
  6. Chang, D.-K.; Chien, T.-L.; Liang, C.-C. Solution Conformation of HIV-1 gp120 Fragment (397-440) by two Dimensional 1H and 13C NMR Spectroscopy and Molecular Modeling. Proceedings of 35th ENC Conference, Pacific Grove, CA, U.S., 1994.
  7. Chang, D. K.; Cheng, S. F.; Chien, W. J.; Liang, C. C. Secondary Structure Change of HIV-1 gp120 Peptide (413-456) Induced by Solvent and Interaction with a Peptide from CD4 Domain 1: Implication on the Mechanism of Fusion between HIV-1 and Its Target Cells. J. Cell. Biochem. 1995, S-21B, 43.
  8. Chang, D. K.; Cheng, S. F.; Chien, W. J.; Chen, S. T.; Liang, C. C. Conformat?ional Study of HIV-1 gp120 Peptide (413-456) by Two Dimensional NMR and Circular Dichroism Studies: Implication on the Mechanism of Fusion between HIV-1 and Its Target Cells. Frontier NMR Research Symposium, Taipei, Taiwan, March, 1995.
  9. Chang, D. K.; Chien, W. J.; Cheng, S. F. Spectroscopic Investigation of Secondary Structure Change of a Peptide from C4 Region of HIV-1 gp120. X1 International Conference of AIDS, July, 1996, Vancouver, Canada.
    C.Technical Report
  1. Bhaskaran, R.; Yang, C. C.; Yu, C.; Chang, D. K. Cardiotoxin III: 1H-NMR Resonance Assignments and Solution Structure Determination. in "Recent Advances in Molecular and Biochemical Research on Proteins", 1993.

Update:2016-01-06

Journal Paper
  1. Li TW, Cheng SF, Tseng YT, Yang YC, Liu WC, Wang SC, Chou MJ, Lin YJ, Wang Y, Hsiao PW, Wu SC, Chang DK Development of single-chain variable fragments (scFv) against influenza virus targeting hemagglutinin subunit 2 (HA2).. Archives of virology 2015-10, 1-13.
  2. Shiuan D, Lin HK, Chen YH, Chang DK, Huang KJ, Farh L Exploration of Peptide Inhibitors of Human Squalene Synthase through Molecular Modeling and Phage Display Technique.. Applied biochemistry and biotechnology 2015-10, 1-12.
  3. Shih-Hung Lin, Ding-Kwo Chang, Mei-Ju Chou, Kao-Jean Huang, David Shiuan* Peptide inhibitors of human HMG-CoA reductase as potential. Biochemical and Biophysical Research Communications 2015-01459,04-109.
  4. Cheng SF, Sung TC, Chang CC, Chou MJ, Chiang YW, Chang DK Kinetics Study on the HIV-1 Ectodomain Protein Quaternary Structure Formation Reveals Coupling of Chain Folding and Self-Assembly in the Refolding Cascade.. Journal of Physical Chemistry B 2014-11118(45), 12827-36.
  5. Yu-Jen Lin, Chia-Ying Wu, Taiwei Li, Pei-Wen Hsiao and Ding-Kwo Chang A rapid and sensitive early diagnosis of influenza virus subtype via SERS. Journal of Biosensors & Bioelectronics 2014-04, 5(2):150.
  6. Lin KC, Chen CY, Chang CW, Huang KJ, Lin SP, Lin SH, Chang DK, Lin MR, Shiuan D A dodecapeptide (YQVTQSKVMSHR) exhibits antibacterial effect and induces cell aggregation in Escherichia coli.. Applied microbiology and biotechnology 2012-0594(3), 755-62.
  7. Wei HJ et al. Fabrication of influenza virus-like particles using M2 fusion proteins for imaging single viruses and designing vaccines . VACCINE 2011-0929, 7163-7172.
  8. Chang, CC etal. Stability of gp41 hairpin and helix bundle assembly probed by combined stacking and circular dichroic approaches . JOURNAL OF STRUCTURAL BIOLOGY 2011-09175, 406-414.
  9. Lin, Chi-Hui et al. An efficient production and characterization of HIV-1 gp41 ectodomain with fusion peptide in Escherichia coli system. JOURNAL OF BIOTECHNOLOGY 2011-04153, 48-55.
  10. Yi-Shin Pan, Hung-JuWei, Chung-Chieh Chang,1 Chung-Hung Lin,e Ting-ShyangWei, Suh-ChinWu and Ding-Kwo Chang Construction and Characterization of Insect Cell-Derived Influenza VLP: Cell Binding, Fusion, and EGFP Incorporation. JOURNAL OF BIOMEDICINE AND BIOTECHNOLOGY 2010-10Article ID 506363, 11 pages.
  11. Cheng SF, Chien MP, Lin CH, Chang CC, Lin CH, Liu YT, Chang DK The fusion peptide domain is the primary membrane-inserted region and enhances membrane interaction of the ectodomain of HIV-1 gp41.. Molecular membrane biology 2010-0127(1), 32-49.
  12. Miao-Ping Chien, Chi-Hui Lin and Ding-Kwo Chang Recruitment of HIV-1 Envelope Occurs Subsequent to Lipid Mixing: A Fluorescence Microscopic Evidence. Retrovirology. RETROVIROLOGY 2009-03, 6:20.
  13. Chen SS, Yang P, Ke PY, Li HF, Chan WE, Chang DK, Chuang CK, Tsai Y, Huang SC Identification of the LWYIK motif located in the human immunodeficiency virus type 1 transmembrane gp41 protein as a distinct determinant for viral infection.. Journal of virology 200983(2), 870-83.
  14. Kantchev EA, Chang CC, Cheng SF, Roche AC, Chang DK Direct solid-phase synthesis and fluorescence labeling of large, monodisperse mannosylated dendrons in a peptide synthesizer.. Organic & biomolecular chemistry 20086(8), 1377-85.
  15. Chang DK, Cheng SF, Kantchev EA, Lin CH, Liu YT Membrane interaction and structure of the transmembrane domain of influenza hemagglutinin and its fusion peptide complex.. BMC biology 20086, 2.
  16. Lin CH, Chang CC, Cheng SF, Chang DK The application of perfluorooctanoate to investigate trimerization of the human immunodeficiency virus-1 gp41 ectodomain by electrophoresis.. Electrophoresis 200829(15), 3175-82.
  17. Chien MP, Jiang S, Chang DK The function of coreceptor as a basis for the kinetic dissection of HIV type 1 envelope protein-mediated cell fusion.. FASEB JOURNAL 200822(4), 1179-92.
  18. Chang DK, Hsu CS Biophysical evidence of two docking sites of the carboxyl heptad repeat region within the amino heptad repeat region of gp41 of human immunodeficiency virus type 1.. Antiviral research 200774(1), 51-8.
  19. Kantchev EA, Chang CC, Chang DK Direct Fmoc/tert-Bu solid phase synthesis of octamannosyl polylysine dendrimer-peptide conjugates.. Biopolymers 200684(2), 232-40.
  20. Chang DK, Cheng SF pH-dependence of intermediate steps of membrane fusion induced by the influenza fusion peptide.. The Biochemical journal 2006396(3), 557-63.
  21. Chang DK, Cheng SF, Lin CH, Kantchev EB, Wu CW Self-association of glutamic acid-rich fusion peptide analogs of influenza hemagglutinin in the membrane-mimic environments: effects of positional difference of glutamic acids on side chain ionization constant and intra- and inter-peptide interactions deduced from NMR and gel electrophoresis measurements.. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES 20051712(1), 37-51.
  22. Kantchev EA, Cheng SF, Wu CW, Huang HJ, Chang DK Secondary structure, phospholipid membrane interactions, and fusion activity of two glutamate-rich analogs of influenza hemagglutinin fusion peptide.. Archives of biochemistry and biophysics 2004425(2), 173-83.
  23. Cheng SF, Wu CW, Kantchev EA, Chang DK Structure and membrane interaction of the internal fusion peptide of avian sarcoma leukosis virus.. EUROPEAN JOURNAL OF BIOCHEMISTRY 2004271(23-24), 4725-36.
  24. Wu CW, Cheng SF, Huang WN, Trivedi VD, Veeramuthu B, Assen B K, Wu WG, Chang DK Effects of alterations of the amino-terminal glycine of influenza hemagglutinin fusion peptide on its structure, organization and membrane interactions.. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES 20031612(1), 41-51.
  25. Cheng SF, Kantchev AB, Chang DK Fluorescence evidence for a loose self-assembly of the fusion peptide of influenza virus HA2 in the lipid bilayer.. Molecular membrane biology 200320(4), 345-51.
  26. Trivedi VD, Cheng SF, Wu CW, Karthikeyan R, Chen CJ, Chang DK The LLSGIV stretch of the N-terminal region of HIV-1 gp41 is critical for binding to a model peptide, T20.. PROTEIN ENGINEERING DESIGN & SELECTION 200316(4), 311-7.
  27. Hsu CH, Wu SH, Chang DK, Chen C Structural characterizations of fusion peptide analogs of influenza virus hemagglutinin. Implication of the necessity of a helix-hinge-helix motif in fusion activity.. The Journal of biological chemistry 2002277(25), 22725-33.
  28. Chang DK, Cheng SF, Trivedi VD Conformation and interaction with the membrane models of the amino-terminal peptide of influenza virus hemagglutinin HA2 at fusion pH.. Archives of biochemistry and biophysics 2001396(1), 89-98.
  29. Chang DK, Trivedi VD, Cheng SF, Francis S The leucine zipper motif of the envelope glycoprotein ectodomain of human immunodeficiency virus type 1 contains conformationally flexible regions as revealed by NMR and circular dichroism studies in different media.. JOURNAL OF PEPTIDE RESEARCH 200157(3), 234-9.
  30. Chang DK, Cheng SF, Yang SH A helix initiation motif, XLLRA, is stabilized by hydrogen bond, hydrophobic and van der Waals interactions.. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY 20001478(1), 39-50.
  31. Trivedi VD, Yu C, Veeramuthu B, Francis S, Chang DK Fusion induced aggregation of model vesicles studied by dynamic and static light scattering.. Chemistry and physics of lipids 2000107(1), 99-106.
  32. Samuel D, Kumar TK, Ganesh G, Jayaraman G, Yang PW, Chang MM, Trivedi VD, Wang SL, Hwang KC, Chang DK, Yu C Proline inhibits aggregation during protein refolding.. Protein science : a publication of the Protein Society 20009(2), 344-52.
  33. Chang DK, Ricciardiello L, Goel A, Chang CL, Boland CR Steady-state regulation of the human DNA mismatch repair system.. The Journal of biological chemistry 2000275(24), 18424-31.
Paper of Conference (or Symposium)
  1. Chang, D. K., 2004, “HIV GP fusion with membrane.”, paper presented at The Four Sino-France Symposium on Synthesis of Drugs and Drug-Protein Interaction, Taipei, Taiwan: The Four Sino-France Symposium on Synthesis of Drugs and Drug-Protein Interaction, 2004-05-03.
  2. Chang, D. K., 2001, “Structure and organization of viral transmembrane fusion proteins.”, paper presented at Japan-Taiwan NMR Symposium, Kyoto, Japan: Japan-Taiwan NMR Symposium, 2001-11-12 ~ 2001-11-13.