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Biochemistry Department - Primary Faculty

Qing-xin Hua

Associate Professor


  • B.S: Department of Biophysics, University of Sciences and Technology of China, Beijing in 1963
  • Research: The Institute of Biophysics, Chinese Academy of Sciences, Beijing, 1963-1989
  • Postdoc:
    • 1985: The National Institute for medical Research, MRC, London in 1985 with Prof. G. C. K. Roberts
    • 1987: The Institute of Biophysics and Molecular Biology, ETH-Honggerberg, Zurich, Switzerland in Prof. K. Wuthrich lab

Research Interests

Dr. Hua's research focuses on the solution structure, folding, binding and dynamics of insulin and other proteins by use of NMR and some biophysical-chemistry methods. In addition of “Classical” adult onset of diabetes mellitus, there is new neonatal onset of diabetes, NMR study of which reveals the impair mechanism: either directly prevent the receptor binding or indirectly damage correct folding and disulfide pairing of mutant proinsulin. Our series studies on insulin folding intermediates include three disulfide model (disulfide-swapped insulin) and two disulfides or one disulfide analogs (substitution of Cys by Ala or Ser). The results imply that the “super-secondary structure” is the “folding nucleus” of insulin family. While insulin mutation at putative receptor-binding position by using “convention” amino acid substitution reveal folding, binding and chain combination in detail, the “abnormal” residue such as D-Ala or D-Ser replacement at structural switch position enable to decode T-R transition or even reveal more information of insulin evolution. Our insulin project lasts as long as 20 years, however, the study of insulin still faces new challenge. Final goal is to figure out the conformation and characteristic of receptor-bound insulin and consequently design new insulin analog with more stable, active and easy preparation for clinic.

Selected References

  • Hua QX, Xu B, Huang K, Hu SQ, Nakagawa S, Jia W, Wang SH, Whittaker J, Katsoyannis PG, Weiss MA.
    “Enhancing the activity of a protein by stereospecific unfolding. The conformational life cycle of insulin and its evolutionary origins. ”
    J. Biol. Chem. 2009 Mar 25. [Epub ahead of print] (Selected as “Paper of the week”)
  • Hua QX, Nakagawa SH, Jia W, Huang K, Phillips NB, Hu SQ, Weiss MA.
    “Design of an active ultrastable single-chain insulin analog: synthesis, structure, and therapeutic implications. ”
    J. Biol. Chem. 283:14703-16. (2008) (Selected as “Paper of the week”)
  • Hua QX, Mayer JP, Jia W, Zhang J, Weiss MA.
    “The folding nucleus of the insulin superfamily: a flexible peptide model foreshadows the native state. ”
    J. Biol. Chem. 281:28131-42. (2006)
  • Hua QX, Nakagawa S, Hu SQ, Jia W, Wang S, Weiss MA.
    “Toward the active conformation of insulin: stereospecific modulation of a structural switch in the B chain. ”
    J. Biol. Chem. 281:24900-9. (2006)
  • Hua QX, Liu M, Hu SQ, Jia W, Arvan P, Weiss MA.
    “A conserved histidine in insulin is required for the foldability of human proinsulin: structure and function of an ALAB5 analog.α.”
    J. Biol. Chem. 281:24889-99. (2006)


Qing-xin Hua Faculty's publications at pubmed