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Yujia Xu

Associate Professor
 
Department :
Chemistry
Membership :
Associate Member
Core Research :
General
Office :
Room 1304C North
Email :
Office Phone :
(212) 772-4310
Office Fax :
(212) 772-5332
Lab Room:
Room 1303 North
Lab Phone :
(212) 772-5614
Education :
  • B.S. (Biology), Lanzhou University, P.R. China, 1987
  • Ph.D. (Biophysics), University of Connecticut, Storrs, CT, 1995
Research Interest :

Interaction and molecular recognition of protein, their involvement in diseased state and the applications in nano-technology. Biological functions often depend on the assembling of macromolecules into well-defined networks and complexes. Our research is to use recombinant collagen triple helix as a model system to explore the determining factors that govern the higher level molecular assembly. The related knowledge will lead to the understanding of the molecular basis of tissue functions, the mechanism of macromolecular organizations and how mutations in collagens cause diseases. Recently, through the collaboration with Prof. Matsui and Prof. Francesconi in the Department of Chemistry, we have started to explore a new research direction: develop collagen triple helix as molecular scaffolds for applications in nanotechnology and radio chemistry.

Selected Publications :
  • Bai, H., Xu, K., Xu, Y., Matsui, H. (2007) Fabrication of Au Nanowires of Uniform Length and Diameter Using a Monodisperse and Rigid Biomolecular Template: Collagen-like Triple Helix, Angew. Chem. Int. Ed. Published Online
  • Tsai, M., Xu, Y. and Dannenberg, J. J.,(2005) Completely Geometrically Optimized DFT/ONIOM Triple-Helical Collagen-like Structures Containing the ProProGly, ProProAla, ProProDAla and ProProDSer Triads, J. Am. Chem. Soc. (127):14130-14131
  • Chien, C., Xu, Y., Xiao, Rong., Aramini, J. M., Sahasrabudhe, P. V., Krug, R. M., and Montelione, G. T. (2004) Biophysical Characterization of the Complex Between Double-Stranded RNA and the N-terminal Domain of the NS1 Protein from Influenza A Virus: Evidence for a Novel RNA-Binding Mode, Biochemistry 43, 1950-1962
  • Persikov, A., Xu, Y., Brodsky, B. (2004) The two-state reversible folding and unfolding reaction of collagen triple helical peptides, Protein Sciences, 13:893-902.
  • Xu, Y. (2004) Characterization of heterogeneity of self-associating systems using equilibrium sedimentation techniques, Biophysical Chemistry 108:61-43
  • Xu, Y., Hyde T., Bhate, M., Lu, X., Broadsky, B., and Baum. (2003) NMR and CD Spectroscopy Show that Imino Acid Restriction of the Unfolded State Leads to Efficient Folding, Biochemistry 42, 8696-8703
  • Liu, S., Lu H, Xu, Y., and Jiang, S. (2005) Different from the HIV fusion Inhibitor C34, the Anti-HIV Drug Fuzeon (T-20) Inhibits HIV-1 Entry by Targeting Multiple Sites in gp41 and gp120, J. Biol Chem. 280(12):11259-73
  • Y. Xu*, (2009) Thermal Stability of Collagen Triple Helix, Methods in Enzymology, Vol 466, Biothermodynamics Part B:212-232
  • Xu, K., Nowak, I., Kirchner, M., and Xu*, Y. (2008) Recombinant collagen studies link the severe conformational changes induced by Osteogenesis imperfecta mutations to the disruption of a set of interchain salt-bridges. J. Biol. Chem. 283:34227-34344
  • Tsai, Midas (I-Hsien); Xu, Y.; and Dannenberg*, J., (2008) Ramachandran Revisited. DFT Energy Surfaces of Diastereomeric Trialanine Peptides in the Gas Phase and Aqueous Solution, J. Phys Chem, J. Phys. Chem. B 113:309
  • Bai, H., Xu, K., Xu*, Y., and Matsui*, H., (2007) Fabrication of Au nanowire in uniform length and diameter using a new monodisperse and rigid biomolecular template, collagen triple helix, Accepted, Angewante Chemie 46 (18): 3319-3322 (Selected as the ‘Hot Papers’ by the editor)