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  • 職稱: 副教授
  • 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。我們實驗室目前研究的主題蛋白質廣泛,相關疾病涵蓋漸凍人症、神經退化症、癌症、免疫等。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功能及致病機制。

更多內容請參觀本實驗室網頁 連結


  • Li HR, Chiang WC, Chou PC, Wang WJ, Huang JR*. "TAR DNA-binding protein 43 (TDP-43) liquid-liquid phase separation is mediated by just a few aromatic residues" (2018) J Biol Chem 293(16):6090-6098

  • Li HR, Chen TC, Hsiao CL, Shi L, Chou CY, Huang JR*. "The physical forces mediating self-association and phase-separation in the C-terminal domain of TDP-43." (2018) BBA-Proteins and Proteomics 1866:214-223

  • Lin YH, Qiu DC, Chang WH, Yeh YQ, Jeng US, Liu FT, Huang JR*. "The intrinsically disordered N-terminal domain of galectin-3 dynamically mediates multisite self-association of the protein through fuzzy interactions." (2017) J Biol Chem 292(43) 17845–17856

  • 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

  • Before 2013
  • 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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