台灣光子源興建計畫
台灣光子源實驗設施
光源監控
用戶資訊
安全訓練
科教資源
光源學程
光源產業應用
招待所申請
參觀申請
人才招募
研發替代役役男專區
新聞
活動公告
研究動態
採購招標資訊
資訊公開區

 
科學研究組
姓          名: 陳俊榮( Chun-Jung Chen )
分          機: 7330
電 子 郵 件: cjchen@nsrrc.org.tw
學          歷:
  • 美國匹茲堡大學結晶學系博士 (1994-1999)
  • 國立清華大學生命科學研究所碩士 (1989-1991)
  • 國立清華大學物理系學士 (1985-1989)
經          歷:
  • 國家同步輻射研究中心研究組生命科學小組研究員(2011/01~迄今)
  • 國立成功大學生物科技所合聘教授 (2011/08~)
  • 國立清華大學物理系合聘教授 (2011/08~)
  • 國家同步輻射研究中心研究組生命科學小組副研究員(2004/01~2010/12)
  • 國立成功大學生物科技所合聘副教授 (2008/08~2011/07)
  • 國立清華大學物理系合聘副教授 (2005/08~2011/07)
  • 國立清華大學生命科學院結構生物學程專任教授 (2004/08~)
  • 國家同步輻射研究中心研究組博士級助研究員(2001/01~2003/12)
  • 國立清華大學物理系合聘助理教授 (2002/08~2005/07)
  • 國立清華大學物理系兼任助理教授 (2001/08~2002/07)
  • 美國喬治亞大學生物化學及分子生物學系博士後研究員(1999/12~2000/10)
負責實驗站:
  • 蛋白質結晶學與結構生物學實驗室
  • SPring-8 BL12B2 & BL44XU
研 究 領 域:
  • 研究領域主要為同步輻射蛋白質結晶學、分子生物物理、結構生物學與蛋白質體學。運用生物物理研究相關之生命科學及結晶學設備,配合單晶繞射儀、國家同步輻射研究中心(NSRRC)和日本SPring-8同步加速器之X光及結晶學實驗站,來進行蛋白質及小分子晶體結構與功能研究。實驗室設有生命科學與生物物理研究之分子生物、生化及蛋白質結晶學設備,可進行晶體培養、繞射數據收集、結構解析及功能研究等。除了蛋白質結晶學外,也運用同步輻射小角度X-光繞射 (SAXS)、圓二色光譜(SRCD)X光吸收細微結構(XAFS)等重要方法,針對生命科學醫學農漁業相關重要蛋白質,研究其結構與功能之關係,並提昇在醫藥學、農漁業及生物科技之應用價值。 研究主要可分為幾個方向:
    (一)針對厭氧菌(如
    Desulfovibrio gigas)有關硫代謝過程、氧氣防禦機制中多種蛋白質及小分子結構與功能關係進行系統性的探討,以了解厭氧菌在無氧環境中的生命作用機制,探討這些蛋白質的生理功能及分子結構,將有助於對微生物在醫學、環境、農工業方面的應用。
    (二)針對稻米發芽時在無氧及有氧環境下的細胞生長與鞘葉伸展相關的蛋白質進行結構功能之研究。稻米是目前已知具無氧發育物種中的高等生物,長期計畫將從稻米基因中找出完整的相關功能蛋白質,進行系統性研究,以進一步了解稻米的無氧及有氧發育過程。
    (三)進行國內外相關領域合作,研究重要蛋白質結構及功能之關係,如細胞膜蛋白質、病毒、海生腔腸動物螢光酵素、生物能源關鍵酵素、蘭花與植物相關蛋白質、斑馬魚與魚類蛋白質及病毒、疾病醫學與藥物設計相關蛋白質等結構。透過結構的研究,對其生物功能進一步瞭解如,以解決生物上未知的訊息

    (四)探討發展
    X光繞射蛋白質結晶學基礎理論,特別是繞射數據的相位角問題。利用X光單波長異常散射進行正確相位角計算與相位角誤差改善,以利電子密度圖的計算及晶體結構解析的應用研究。

代   表   作:
  • For the complete list, please go to https://www.researchgate.net/profile/Chun-Jung_Chen2 or http://www.researcherid.com/rid/A-6880-2011 or https://scholar.google.com.tw/citations?user=oTFF8K0AAAAJ&hl=zh-TW
  • Guan, H.-H. Yoshimura, M., Chuankhayan, P., Lin, C.-C., Chen, N.-C., Yang, M.-C., Ismail, A., Fun, H.-K., Chen, C.-J.* Crystal structure of an antigenic outer-membrane protein from Salmonella Typhi suggests a potential antigenic loop and an efflux mechanism” Sci. Rep. (Nature Publishing Group), 5:16441 (2015).
  • Chen, N.-C., Yoshimura, M., Guan, H.-H., Wang, T.-Y., Misumi, Y., Lin, C.-C., Chuankhayan, P., Nakagawa, A., Chan, S. I., Tsukihara, T., Chen, T.-Y., Chen, C.-J.* “Crystal structures of a piscine betanodavirus: mechanisms of capsid assembly and viral infection” PLoS Path. 11(10): e1005203 (2015).
  • Chen, K. H.-C., Chuankhayan, C., Wu, H.-H., Chen, C.-J.*, Fukuda, M., Yu, S. S.-F., Chan, S. I. "The bacteriohemerythrin from Methylococcus capsulatus (Bath): Crystal structures reveal Leu114 regulates the substrate tunnel" J. Inorg. Biochem. 15, 81-89 (2015).
  • Lin, C.-C., Chuankhayan, P., Chang, W.-N., Kao, T.-T., Guan, H.-H., Fun, H.-K., Nakagawa, A., Fu, T.F., Chen, C.-J.* “Crystal structures of the hydrolase domain of zebrafish 10-formyltetrahydrofolate dehydrogenase and its complexes reveal a complete set of key residues for hydrolysis and product Inhibition”, Acta Cryst. D71. 1006-1021 (2015).
  • Chen, C.-D., Huang, Y.-C., Chiang, H.-L., Hsieh, Y.-C., Chuankhayan, P., Chen, C.-J.* “Direct phase selection of initial phases from single-wavelength anomalous dispersion (SAD) for the improvement of electron density and ab initio structure determination” Acta Cryst. D70, 2331-2343 (2014).
  • Praditwongwan, W, Chuankhayan, P., Saoin, S., Wisitponchai, T., Lee, V. S., Nangola, S., Hong, S. S., Minard, P., Boulanger, P., Chen, C.-J.*, Tayapiwatana, C. “Crystal structure of an antiviral ankyrin targeting the HIV-1 capsid and molecular modeling of the ankyrin-capsid complex” J. Comput. Mol. Des. 28, 869-884 (2014).
  • Chuankhayan, P., Tao, T.-T., Lin, C.-C., Guan, H.-H., Nakagawa, A., Fu, T.-F., Chen, C.-J.* “Structural insights into the hydrolysis and polymorphism of methotrexate polyglutamate by zebrafish γ-glutamyl hydrolase” J. Med. Chem. 56, 7625-7635 (2013).
  • Hsieh, Y.-C., Chen, M.-C., Hsu, C.-C., Chan, S. I., Yang, Y.-S., Chen, C.-J.* “Crystal structures of vertebrate dihydropyrimidinase and complexes from Tetraodon Nigroviridis with lysine carbamylation: metal and structural requirements for post-translational modification and function” J. Biol. Chem. 288, 30645-30658 (2013).
  • Tien, Y.-C., Chuakhanyan, P., Huang, Y.-C., Chen, C.-D., Alikhajeh, J., Chang, S.-L., Chen, C.-J.* “Crystal structures of rice (Oryza sativa) glyceraldehyde-3-phosphate dehydrogenase complexes with NAD+ and sulfate suggests involvement of Phe37 in NAD+-specificity”. Plant Mol.Biol. 80, 389-403 (2012).
  • Chen, C.-D., Lin, C.-H., Chuankhayan P., Huang, Y.-C., Hsieh, Y.-C., Huang, T.-F., Guan, H.-H., Liu, M.-Y., Chang, W.-C., Chen, C.-J.* “Crystal structures of complexes of the branched-chain aminotransferase from Deinococcus radiodurans with α-ketoisocaproate and L-glutamate suggest the radiation resistance of this enzyme for catalysis”. J Bacteriol. 194, 6206-6216 (2012).
  • Fang, J.-Y., Chiang, Y.-L., Hsieh, Y.-C., Wang, V. C.-C., Huang, Y.-C., Chuankhayan, P., Liu, M.-Y., Chan, S. I., Chen, C.-J.* “Crystallization of adenylylsulfate reductase from Desulfovibrio gigas: A strategy based on controlled protein oligomerization” Cryst. Growth & Des. 11, 2121-2134 (2011).
  • Hsieh, Y.-C., Liu, M.-Y., Wang, V. C.-C., Chiang Y.-L., Liu, E.-H., Wu, W., Chan, S. I., Chen, C.-J.*Structural insights into the enzyme catalysis from comparison of three forms of dissimilatory sulfite reductase from Desulfovibrio gigasMol. Microbiol. 78, 1101-1116 (2010).
  • Chang, C.-Y., Hsieh, Y.-C., Wang, T.-Y., Chen, Y.-C., Wang Y.-K., Chiang, T.-W., Chen, Y.-J., Chen, C.-J.*, Wu, T.-K. “Crystal structure and mutational analysis of aminoacylhistidine dipeptidase from Vibrio alginolyticus reveal a new architecture of M20 metallopeptidases”, J. Biol. Chem. 285, 39500-39515 (2010).
  • Hsieh, Y.-C., Wu, Y.-J., Chiag, T.-Y., Kuo, C.-Y., Shrestha, K. L., Chao, C.-F., Huang, Y.-C., Chuankhayan, P., Wu, W., Li, Y.-K., Chen, C.-J.* “Crystal structures of Bacillus cereus NCTU2 chitinase complexes with chitooligomers reveal novel substrate binding for catalysis: a chitinase without chitin-binding and insertion domains” J. Biol. Chem. 285, 31603-31615 (2010).
  • Chuankhayan, P., Hsieh, C.-Y., Huang, Y.-C., Hsieh, Y.-Y., Guan, H.-H., Hsieh, Y.-C., Tien, Y.-C., Chen, C.-D., Chiang, C.-M., Chen, C.-J.* “Crystal structures of Aspergillus japonicus fructosyltransferase complex with donor/acceptor substrates reveal complete subsites in the active site for catalysis” J. Biol. Chem. 285, 23249-23262 (2010).
  • Guan, H.-H. Guan, Goh, K.-S., Davamani, F., Wu, P.-L., Huang, Y.-W., Jeyakanthan, J., Wu, W., Chen, C.-J.* “Structures of two elapid snake venom metalloproteases with distinct activities highlight the disulfide patterns in the D domain of ADAMalysin family proteins”, J. Struct. Biol. 169, 294-303 (2010).
  • Chiang, Y.-L., Hsieh, Y.-C., Fang, J.-Y., Liu, E.-H., Huang, Y.-C., Chuankhayan, P., Jeyaraman, J., Liu, M.-Y., Chan, S. I., Chen, C.-J.* “Crystal structure of adenylylsulfate reductase from Desulfovibrio gigas suggests a potential self-regulation mechanism involving the C-terminus of the β-subunit”. J. Bacteriol. 191, 7597-7608 (2009).
  • Yang, M.-C., Guan, H.-H., Liu, M.-Y., Lin, Y.-H., Yang, J.-M., Chen, W.-L., Chen, C.-J.*, Mao, S.J.T. “Rational design for crystallization of b-Lactoglobulin and vitamin D3 complex: revealing a secondary binding site”, Cryst. Growth and Des. 8, 4268-4276 (2008).
  • Yang, M.-C., Guan, H.-H., Liu, M.-Y., Lin, Y.-H., Yang, J.-M., Chen, W.-L., Chen, C.-J.*, Mao, S.J.T. “Crystal structure of a secondary vitamin D3 binding site of milk b-lactoglobulin”, Proteins, 71, 1197-1210 (2008).
  • Elmi, F., Lee, H.-T., Huang, J.-Y., Hsieh, Y.-C., Wang, Y.-L., Chen, Y.-J., Shaw, S.-Y., Chen C.-J.* “Stereoselective esterase from Pseudomonas putida reveals an a/b hydrolase fold for D-b  acetylthioisobutyric acid synthesis”, J. Bacteriol. 187, 8470-8476 (2005).
  • Huang, J.-Y, Chang, T, Chang, C.-Y., Chen, C.-J.* “Crystal structure of a nucleoside diphosphate kinase required for coleoptile elongation in rice (Oryza sativa L.)”, J. Strut. Biol. 150, 309-318 (2005).
  • Lee, S.-C., Guan, H.-H., Wang, C.-H., Huang, W.-N., Chen, C.-J.*, and Wu, W. “Structural basis of venom citrate-dependent heparan sulfate-mediated cell surface retention of cobra cardiotoxin A3”. J. Biol. Chem. 280, 9567-9577 (2005).