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Huang, Jie-rong
 黃介嶸老師
  • Education : PhD. Univ. of Cambridge (Dept. of Chemistry); BSc. National Taiwan Univ. (Dept. of Physics)
  • Office : R607, 6F, Tradition Medicine Building
  • Phone: 886-2-28267258
  • Email: jierongh@ym.edu.tw
  • Personal Web Site :http://www.ym.edu.tw/~jierongh/
  • Research

    It is generally accepted that many functional proteins do not have well-defined folded structures. These so-called intrinsically disordered proteins (IDPs) are encoded abundantly in the human genome and are involved in a variety of biological process including cell signalling, cell cycle control, molecular recognition, nucleic acid transcription and replication, as well as the development of neurodegenerative diseases and cancer. The studies of IDPs is an emerging field of research and general rules for describing their conformational behaviour and mechanisms are still missing. Thus, expanding the amount of experimental data from different systems as well as developing new techniques to characterize their properties are essential to improve our knowledge about this family of proteins.

    We are interested in using state-of-the-art nuclear magnetic resonance techniques and other biophysical methods in combination with novel computational modelling to explore the structural propensity and dynamics of IDPs and the mechanism of their interaction with other proteins or nucleic acids at atomic resolution.


    Publication

    • 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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