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  • 職稱: 助理教授
  • 學歷:PhD. Univ. of Cambridge (Dept. of Chemistry); BSc. National Taiwan Univ. (Dept. of Physics)
  • 經歷: Postdoc. University of Basel, Switzerland; Postdoc. CNRS, France
  • 辦公室: 傳醫乙棟 六樓 R607 室
  • 電話: 886-2-2826-7258
  • Email:
  • 個人網頁:


在人體中,35%以上的蛋白質並無完整的三維結構但卻保有其生物功能,這類蛋白質稱為固有無序蛋白質(intrinsically disordered proteins)。此類蛋白質除了在生物體內的反應,如:信號傳遞、細胞週期調控、生物分子辨識、DNA的轉錄與複製,佔有重要角色外,它們和神經退化性疾病,如:阿茲海默症及帕金森氏症,也密切相關。我們實驗室目前主要的研究主題包含和漸凍人症與神經退化症相關的TDP-43及和癌症、免疫、發炎反應相關的Galtin-3。我們希望藉由生物化學及生物物理的實驗技術,從分子的層級去了解這類蛋白質的致病機制。

更多內容請參觀本實驗室網頁 連結


  • Chen TC, Hsiao CL, Huang SJ, Huang JR*. The nearest-neighbor effect on random-coil NMR chemical shifts demonstrated using a low-complexity amino-acid sequence. (2016) Protein Pept Lett. 23(11):967-975


  • Delaforge E, Milles S, Huang JR, Bouvier D, Jensen MR, Sattler M, Hart JD, Blackledge M. Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions. (2016) Front. Mol. Biosci. 3:54


  • Aznauryan M, Delgado L, Soranno A, Nettels D, Huang JR, Labhardt AM, Grzesiek S, Schuler B. Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR, and SAXS. (2016) PNAS 113(37):E5389-98


  • Huang JR, Warner LR, Sanchez C, Gabel F, Madl T, Mackereth CD, Sattler M, Blackledge M. Transient electrostatic interactions dominate the conformational equilibrium sampled by multi-domain splicing factor U2AF65: A combined NMR and SAXS study. (2014) J Am Chem Soc 136(19):7068-76


  • Jensen MR, Zweckstetter M, Huang JR, Blackledge M. Exploring Free-Energy Landscapes of Intrinsically Disordered Proteins at Atomic Resolution Using NMR Spectroscopy. (2014) Chem Rev 114(13):6632-60


  • Huang J-R, Ozenne V, Jensen MR, and Blackledge M. Direct prediction of NMR residual dipolar couplings from the primary sequence of unfolded proteins  (2013) Angew Chem Int Ed 52(2):687-690 (Cover Issue)


  • Huang J-R, Gentner M, Vajpai N, Grzesiek S, and Blackledge M. Residual dipolar couplings measured in unfolded proteins are sensitive to amino- acid specific geometries as well as local conformational sampling (2012) Biochem Soc T 40(5):989-94


  • Ozenne V, Schneider R, Yao M, Huang J-R, Salmon L, Zweckstetter M, Jensen MR and Blackledge M. Mapping the potential energy landscape of intrinsically disordered proteins at amino acid resolution (2012) J Am Chem Soc 134(36):15138-48


  • Ozenne V, Bauer F, Salmon L, Huang J-R, Jensen MR, Segard S, Bernado P, Charavay C, and Blackledge M. Flexible-meccano: A tool for the generation of explicit ensemble description of intrinsically dis- ordered proteins and their associated experimental observables (2012) Bioinfomatics 28(11):1463-70


  • Silvers R, Sziegat F, Tachibana H, Segawa S, Whittaker S, Gunther U, Gabel F, Huang J-R, Blackledge M, Wirmer J, and Schwalbe H. Modulation of structure and dynamics by disulfide bond formation in unfolded states. (2012) J Am Chem Soc 134(15):6846-54


  • Huang J-R, Gabel F, Jensen MR, Grzesiek S, and Blackledge M. Sequencespecific mapping of the interaction between urea and unfolded ubiquitin from ensemble analysis of NMR and small angle scattering data. (2012) J Am Chem Soc 134(9):4429-36


  • Schneider R, Huang J-R, Yao M, Communie G, Ozenne V, Mollica L, Salmon L, Jensen MR, and Blackledge M. Towards a robust descrip- tion of intrinsic protein disorder using nuclear magnetic resonance spec- troscopy. (2012) Mol Biosyst 8(1):58-68


  • Vajpai N, Gentner M, Huang J-R, Blackledge M, and Grzesiek S. Sidechain χ1 conformations in urea-denatured ubiquitin and protein G from 3J coupling constants and residual dipolar couplings. (2010) J Am Chem Soc 132(9):3196-203


  • Huang J-R and Grzesiek S. Ensemble calculations of unstructured proteins constrained by RDC and PRE data: a case study of urea-denatured ubiquitin. (2010) J Am Chem Soc 132(2):694-705


  • Haussinger D, Huang J-R, and Grzesiek S. DOTA-M8–an extremely rigid, high-affinity lanthanide chelating tag for PCS NMR. (2009) J Am Chem Soc 131(41):14761-7


  • Huang J-R, Hsu S-TD, Christodoulou J, and Jackson SE. The extremely slow-exchanging core and acid-denatured state of Green Fluorescent Pro- tein. (2008) HFSP Journal 2(6):378-87


  • Huang J-R, Craggs TD, Christodoulou J, and Jackson SE. Stable intermediate states and high energy barriers in the unfolding of GFP. (2007) J Mol Biol 370(2):356-71


  • Jackson SE, Craggs TD, Huang J-R. Understanding the folding of GFP using biophysical techniques. (2006) Expert Rev Proteomics 3(5):545-59
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