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Yujia Xu, Ph.D.

Associate Professor - Biophysical Chemistry


Contact Information:

office 1304cN (tel 212-772-4310), lab 1303N (tel 212-772-5614), dept fax 212-772-5332, email

Research Summary: 

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. About twenty different types of collagen molecules have been identified in humans, occurring in almost every tissue. Different types of collagen share the same basic structure unit – the triple helix, consisting of three poly-peptide chains with the characteristic (Gly-X-Y)n repeating (amino acid) sequence. The triple helix further assembles into different supramolecular structures that confer the diverse biological properties of different tissues. Understanding of the mechanism of molecular assembly of collagen will be essential for our understanding of the molecular basis of tissue functions, the mechanism of macromolecular organizations and how mutations in collagens cause diseases.

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

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

Xu, Y. (2004) Characterization of heterogeneity of self-associating systems using equilibrium sedimentation techniques, Biophysical Chemistry 108:61-43

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.

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

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