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Please send your questions, requests, and comments to:

Hongjun Zhou, Ph.D.

Sr. Development Engineer & Director
NMR Facility
Department of Chemistry and Biochemistry
University of California
Santa Barbara, CA 93106-9510

E-mail: hzhou@chem.ucsb.edu

Phone: 805-893-2938

Office: PSB North Room 3614A

Hongjun

Publications

  1. Wang X1, Vallurupalli P, Vu A, Lee K, Sun S, Bai WJ, Wu C, Zhou H, Shea JE, Kay LE, Dahlquist FW (2014) The linker between the dimerization and catalytic domains of the CheA histidine kinase propagates changes in structure and dynamics that are important for enzymatic activity. Biochemistry 53, 855-861.
  2. Ortega DR1, Mo G, Lee K, Zhou H, Baudry J, Dahlquist FW, Zhulin IB (2013) Conformational coupling between receptor and kinase binding sites through a conserved salt bridge in a signaling complex scaffold protein. PLoS Comput Biol November 14, 2013.
  3. Matje DM, Zhou H, Smith DA, Neely RK, Dryden DT, Jones AC, Dahlquist FW, Reich NO. (2013) Enzyme-Promoted Base Flipping Controls DNA Methylation Fidelity. Biochemsitry 52, 1677-1685.
  4. Mo G, Zhou H, Kawamura T, Dahlquist FW. (2012) Solution structure of a complex of the histidine autokinase CheA with its substrate CheY. Biochemistry 51, 3786-3798.
  5. Levenson R, Zhou H, Dahlquist FW. (2012) Structural insights into the interaction between the bacterial flagellar motor proteins FliF and FliG. Biochemistry 51, 5052-5060.
  6. Gauglitz, J.M., Zhou, H., & Butler, A. (2012) A suite of citrate-derived siderophores from a marine Vibrio species isolated following the Deepwater Horizon oil spill. J. Inorg. Biochem. 107, 90-95.
  7. Vu, A., Wang, X., Zhou, H., & Dahlquist, F.W. (2012) The receptor-CheW binding interface in bacterial chemotaxis. J. Mol. Biol. 415, 759-767.
  8. Vu, A., Hamel, D.J., Zhou, H., & Dahlquist, F.W. (2011). The structure and dynamic properties of the complete histidine phosphotransfer domain of the chemotaxis specific histidine autokinase CheA from Thermotoga maritima. J. Biomol. NMR 51, 49-55.
  9. Kawamura, T., Vartanian, A.S., Zhou, H., & Dahlquist, F.W. (2011) The design involved in PapI and Lrp regulation of the pap operon. J. Mol. Biol. 409, 311-332.
  10. Mealman, T.D., Bagai, I., Singh, P., Goodlett, D.R., Rensing, C., Zhou, H., Wysocki, V.H., & McEvoy, M.M. (2011) Interactions between CusF and CusB identified by NMR spectroscopy and chemical cross-linking coupled to mass spectrometry. Biochemistry 50, 2559-2566.
  11. Peterson, D.W., Ando, D.M., Taketa, D.A., Zhou, H., Dahlquist, F.W., & Lew, J. (2010) No difference in kinetics of tau or histone phosphorylation by CDK5/p25 versus CDK5/p35 in vitro. Proc. Natl. Acad. Sci. U S A. 207, 2884-2889.
  12. Zhou, H., Purdy, M.M., Dahlquist, F.W., & Reich, N.O. (2009) The recognition pathway for the DNA cytosine methyltransferase M.HhaI. Biochemistry 48, 7807-7816.
  13. Hao, S., Hamel, D., Zhou, H., & Dahlquist, F.W. (2009) Structural basis for the localization of the chemotaxis phosphatase CheZ by CheAS. J. Bacteriol. 18, 5842-5844
  14. Dyer, C.M., Vartanian, A.S., Zhou, H., & Dahlquist, F.W. (2009) A molecular mechanism of bacterial flagellar motor switching. J. Mol. Biol. 388, 71-84.
  15. Peterson, D.W., Zhou, H., Dahlquist, F.W., & Lew, J. (2008) A soluble oligomer of tau associated with fiber formation analyzed by NMR. Biochemistry 47, 7393-7404.
  16. Zhou. H., Shatz, W., Fera, N., Purdy, M.M., Dahlquist, F.W., & Reich, N.O. (2007) Long-range structural and dynamical changes induced by cofactor binding in DNA methyltransferase M.HhaI. Biochemistry 46, 7261-7268.
  17. Kawamura, T., Le, L.U., Zhou, H., & Dahlquist, F.W. (2007) Solution structure of Escherichia coli PapI, a key regulator of the Pap pili phase variation. J. Mol. Biol. 365, 1130-1142.
  18. Hamel, D.J., Zhou, H., Starich, M.R., Byrd, R.A., & Dahlquist, F.W. (2006) Chemical-shift-perturbation mapping of the phosphotransfer and catalytic domain interaction in the histidine autokinase CheA from Thermotoga maritima. Biochemistry 45, 9509-9517.
  19. Daughdrill, G.W., Vise, P.D., Zhou, H., Yang, X., Yu, W.F., Tasayco, M.L., & Lowry, D.F. (2004) Reduced spectral density mapping of a partially folded fragment of E. coli thioredoxin. J. Biomol. Struct. Dyn. 21, 663-670.
  20. Zhou, H., Gallina, M., Mao, H., Nietlispach, D., Betz, S.F., Fetrow, J.S., & Domaille, P.J. (2003) 1H, 13C and 15N resonance assignments and secondary structure of the human protein tyrosine phosphatase, PRL-2. J. Biomol. NMR 27, 397-398.
  21. Griswold, I.J, Zhou, H., Swanson, R.V,, McIntosh, L.P., Simon, M.I., & Dahlquist, F.W. (2002) The solution structure and interactions of chew from thermotoga maritima. Nat. Struct. Biol. 9, 121-125.
  22. Zhou, H., Vermeulen, A., Jucker, F. & Pardi, A. (2001) Incorporating residual dipolar couplings into the NMR solution structure determination of nucleic acids. Biopolymers 52, 168-80.
  23. Vermeulen, A., Zhou, H. & Pardi, A. (2000) Determining DNA global structure and DNA bending by application of NMR dipolar couplings. J. Am. Chem. Soc. 122, 9638-9647.
  24. Zhou, H., Casas-Finet, J.R., Heath Coats, R., Kaufman, J.D., Stahl, S.J., Wingfield, P.T., Rubin, J.S., Bottaro, D.P., & Byrd, R.A. (1999) Identification and dynamics of a heparin-binding site in hepatocyte growth factor. Biochemistry 38, 14793-802.
  25. Chirdadze, D.Y., Hepple, J.P., Zhou, H., Byrd, R.A., Blundell, T.L. & Gherardi, E. (1999) The crystal structure of a receptor-binding fragment of HGF/SF (NK1) suggests a novel mode for growth factor dimerization and receptor binding. Nat. Struct. Biol. 6, 72-78.
  26. Bertelson, E.B., Zhou, H., Lowry, D., Flynn, G.C., & Dahlquist, F.W. (1999) Topology and dynamics of the 10 kDa C-terminal domain of DnaK in solution. Protein Sci. 8, 343-354.
  27. Zhou, H., Mazzulla, M.J., Stahl, S.J., Wingfield, P.T., Rubin, J.S., Bottaro, D.P., & Byrd, R.A. (1998) The solution structure of the N-terminal domain of hepatocyte growth factor reveals a potential heparin-binding site. Structure 6, 109-116
  28. Altieri, A.S., Mazzulla, M.J., Zhou, H., Costantino, N., Court, D. & Byrd, R.A. (1997) Sequential assignments and secondary structure of the RNA-binding transcriptional regulator NusB. FEBS Letters 415, 221-226.
  29. Zhou, H. & Dahlquist, F.W. (1997) The phosphotransfer site of the chemotaxis-specific histidine autokinase CheA as revealed by NMR. Biochemistry 36, 699-710.
  30. Zhou, H., McEvoy, M.M., Lowry, D.F., Swanson, R.V., Simon, M. I. & Dahlquist, F.W. (1996) The phosphotransfer domain and the CheY-binding domain of the histidine kinase CheA are joined by a flexible linker. Biochemistry 35, 433-443.
  31. McEvoy, M.M., Zhou, H., Roth, A.F., Lowry, D.F., Morrison, T.B., Kay, L.E., & Dahlquist, F. W. (1995) Nuclear magnetic resonance assignments and global fold of a CheY-binding domain in CheA, the chemotaxis-specific kinase of Escherichia coli. Biochemistry 34, 13871-13880.
  32. Zhou, H., Lowry, D.F., Swanson, R.V., Simon, M.I., & Dahlquist, F.W. (1995) NMR studies of the phosphotransfer domain of the histidine kinase CheA from Escherichia coli: assignments, secondary structure, general fold, and backbone dynamics. Biochemistry 34, 13858-13870.