Cell and Molecular Biology Programme, The Chinese University of Hong Kong

Prof. WONG, Kam Bo

Address:	Rm. 507B, Mong Man Wai Building, CUHK (Office)
	Rm. 507E Mong Man Wai Building, CUHK(Lab)
Phone:	(852)-26098024 (Off) /(852)-26098073 (Lab)
Fax:	(852)-26037732
E-mail:	kbwong@cuhk.edu.hk

Education

1997	Ph.D. University of Cambridge, UK
1993	M.Phil. The Chinese Unviersity of Hong Kong, Hong Kong
1990	B.Sc. The Chinese University of Hong Kong, Hong Kong

Position

2008-present	Professor (Department of Biochemistry, The Chinese University of Hong Kong)
2003-2008	Associate Professor (Department of Biochemistry, The Chinese University of Hong Kong

1999-2003	Assistant Professor (Department of Biochemistry, CUHK)Assistant Professor (Dept. of Biochemistry, CUHK)


Concurrent Position
2008-present	Associate Director, MBT programme

Professional Activities:

Editorial Board:
2004-present	Protein Engineering, Design and Selection

Research Interest

1.	Structure determination of proteins by NMR spectroscopy and X-ray crystallography
2.	Protein engineering and design
3..	Simulation and molecular modeling of proteins

Representative Publications

1.	Too, P.H., Ma, M.K., Mak, A.N., Wong, Y.T., Tung, C.K., Zhu, G., Au, S.W., Wong, K.B. and Shaw, P.C. (2009) The C-terminal fragment of the ribosomal P protein complexed to trichosanthin reveals the interaction between the ribosome-inactivating protein and the ribosome. Nucleic Acids Res, 37, 602-610.
2.	Tang, W.K., Wong, K.B., Lam, Y.M., Cha, S.S., Cheng, C.H. and Fong, W.P. (2008) The crystal structure of seabream antiquitin reveals the structural basis of its substrate specificity. FEBS Lett, 582, 3090-3096..
3.	Mak, A.N., Wong, Y.T., An, Y.J., Cha, S.S., Sze, K.H., Au, S.W., Wong, K.B. and Shaw, P.C. (2007) Structure-function study of maize ribosome-inactivating protein: implications for the internal inactivation region and the sole glutamate in the active site. Nucleic Acids Res, 35, 6259-6267.
4.	Chan, D.S., Chu, L.O., Lee, K.M., Too, P.H., Ma, K.W., Sze, K.H., Zhu, G., Shaw, P.C. and Wong, K.B. (2007) Interaction between trichosanthin, a ribosome-inactivating protein, and the ribosomal stalk protein P2 by chemical shift perturbation and mutagenesis analyses. Nucleic Acids Res, 35, 1660-1672.
5.	Lee, K.M., Ma, K.W., Shaw, P.C. and Wong, K.B. (2006) A high-yield one-step purification method using copper-chelating chromatography for recombinant proteins fused with maltose-binding protein. Anal Biochem, 358, 152-154.
6.	Lee, C.F., Makhatadze, G.I. and Wong, K.B. (2005) Effects of charge-to-alanine substitutions on the stability of ribosomal protein L30e from Thermococcus celer. Biochemistry, 44, 16817-16825.
7.	Lee, C.F., Allen, M.D., Bycroft, M. and Wong, K.B. (2005) Electrostatic interactions contribute to reduced heat capacity change of unfolding in a thermophilic ribosomal protein l30e. J Mol Biol, 348, 419-431.
8.	Cheung, Y.Y., Lam, S.Y., Chu, W.K., Allen, M.D., Bycroft, M. and Wong, K.B. (2005) Crystal structure of a hyperthermophilic archaeal acylphosphatase from Pyrococcus horikoshii--structural insights into enzymatic catalysis, thermostability, and dimerization. Biochemistry, 44, 4601-4611.
9.	Ip, D.T., Chan, S.H., Allen, M.D., Bycroft, M., Wan, D.C. and Wong, K.B. (2004) Crystallization and preliminary crystallographic analysis of a novel orange fluorescent protein from the Cnidaria tube anemone Cerianthus sp. Acta Crystallogr D Biol Crystallogr, 60, 340-341.
10.	Wong, K.B., Lee, C.F., Chan, S.H., Leung, T.Y., Chen, Y.W. and Bycroft, M. (2003) Solution structure and thermal stability of ribosomal protein L30e from hyperthermophilic archaeon Thermococcus celer. Protein Sci, 12, 1483-1495.
11.	Chen, Y.W., Bycroft, M. and Wong, K.B. (2003) Crystal structure of ribosomal protein L30e from the extreme thermophile Thermococcus celer: thermal stability and RNA binding. Biochemistry, 42, 2857-2865.
12.	Kazmirski, S.L., Wong, K.B., Freund, S.M., Tan, Y.J., Fersht, A.R. and Daggett, V. (2001) Protein folding from a highly disordered denatured state: the folding pathway of chymotrypsin inhibitor 2 at atomic resolution. Proc Natl Acad Sci U S A, 98, 4349-4354.
13.	Wong, K.B., Clarke, J., Bond, C.J., Neira, J.L., Freund, S.M., Fersht, A.R. and Daggett, V. (2000) Towards a complete description of the structural and dynamic properties of the denatured state of barnase and the role of residual structure in folding. J Mol Biol, 296, 1257-1282.
14.	Nikolova, P.V., Wong, K.B., DeDecker, B., Henckel, J. and Fersht, A.R. (2000) Mechanism of rescue of common p53 cancer mutations by second-site suppressor mutations. EMBO J, 19, 370-378.
15.	Wong, K.B., DeDecker, B.S., Freund, S.M., Proctor, M.R., Bycroft, M. and Fersht, A.R. (1999) Hot-spot mutants of p53 core domain evince characteristic local structural changes. Proc Natl Acad Sci U S A, 96, 8438-8442.
16.	Wong, K.B. and Daggett, V. (1998) Barstar has a highly dynamic hydrophobic core: evidence from molecular dynamics simulations and nuclear magnetic resonance relaxation data. Biochemistry, 37, 11182-11192.
17.	Wong, K.B., Fersht, A.R. and Freund, S.M. (1997) NMR 15N relaxation and structural studies reveal slow conformational exchange in barstar C40/82A. J Mol Biol, 268, 494-511.
18.	Bond, C.J., Wong, K.B., Clarke, J., Fersht, A.R. and Daggett, V. (1997) Characterization of residual structure in the thermally denatured state of barnase by simulation and experiment: description of the folding pathway. Proc Natl Acad Sci U S A, 94, 13409-13413.
19.	Wong, K.B., Freund, S.M. and Fersht, A.R. (1996) Cold denaturation of barstar: 1H, 15N and 13C NMR assignment and characterisation of residual structure. J Mol Biol, 259, 805-818.
20.	Freund, S.M., Wong, K.B. and Fersht, A.R. (1996) Initiation sites of protein folding by NMR analysis. Proc Natl Acad Sci U S A, 93, 10600-10603.
21.	Wong, K.B., Ke, Y.B., Dong, Y.C., Li, X.B., Guo, Y.W., Yeung, H.W. and Shaw, P.C. (1994) Structure/function relationship study of Gln156, Glu160 and Glu189 in the active site of trichosanthin. Eur J Biochem, 221, 787-791.

Research Grants

UGC Special Equipment Grant
2008-2011	Acquiring a high field NMR spectrometer for chemical and structural biology – from macromolecular structures and dynamics to biomolecular interaction. HK$10,000,000.

Research Grants Council (RGC) Earmarked Grants
2008-2009	Does charge-charge interaction contribute more to protein stability at high temperatures? – HK$639,261.
2007-2008	Structure-function of hydrogenase maturation factor B (HypB) – structure determination of HypB by X-ray crystallography. HK$654,500.
2006-2009	Is the reduced catalytic efficiency of a thermophilic acylphosphatase a necessary consequence of enhanced stability and rigidity? HK$1,290,183.
2003-2007	Structure-function study of ribosomal protein P2 – structure determination of human P2 by NMR spectroscopy. HK$1,491,000.
2002-2006	Structural basis of thermostability of proteins – protein engineering of a thermophilic protein from a hyperthermophilic Archaeon Thermococcus celer. HK$1,394,000.
2000-2003	Structure-function of a novel RNA- binding motif - structure determination of a ribosomal protein L30e from Thermococcus celer by multi-dimensional NMR spectroscopy. HK$1,015,200

Research Fund for the Control of Infestious Diseases
2007-2008	Substrate specificity and rational design of peptidomimetic inhibitors for SARS coronavirus main protease. HK$775,008