Assistant Professor, Department of Biology
Rensselaer Polytechnic Institute

Education:
Ph.D., Biochemistry and Molecular Genetics, Cornell University, 2000
M.D., Peking Union Medical College (PUMC), 1996
B.S., Premedical Studies, Beijing University, 1991

Career Highlights:
Wang joined the Rensselaer faculty as an assistant professor in 2004 after completing his postdoctoral training in the Department of Biochemistry and Molecular Biophysics at Columbia University.

His many honors and fellowships include a National Research Service Award (NRSA) from the National Institutes of Health (NIH) in 2003, an NIH Endocrine Training Grant Fellowship in 2002, and a Liu and Wu Memorial Fellowship from Cornell University in 1998. Wang was the recipient of a highly competitive Olin Presidential Fellowship from Cornell University in 1997. While, at Peking Union Medical College, he also received an exchange student scholarship to attend the University of California, San Francisco (UCSF) School of Medicine for two months.

Wang’s professional society memberships include American Association for the Advancement of Science, Biophysical Society, American Chemical Society, and American Society for Biochemistry and Molecular Biology.

Research Areas:
Wang’s research focuses on the application of nuclear magnetic resonance (NMR) spectroscopy to study significant and interesting problems in neuroscience and aging, such as Alzheimer’s disease, the most common form of senile dementia.

Membrane proteins are responsible for transmembrane signaling, energy generation and transduction, transmembrane transport, and intramembrane proteolysis. Membrane proteins constitute roughly one-third of the proteome but less than 0.2% of all solved protein structures. This is mainly due to the extreme difficulty in obtaining membrane protein crystals. Solution nuclear magnetic resonance (NMR) spectroscopy circumvents the need for crystallization and plays a prominent role in obtaining structural information of membrane proteins. Wang’s group is studying the structures of key membrane proteins in the pathogenesis of Alzheimer’s disease.

Static protein structures alone often cannot explain the mechanisms of protein function, because protein function, such as folding, recognition, catalysis, energy generation and transduction, and transport, invariably involves protein motion. Solution NMR is the most powerful technique for studying protein dynamics. Wang’s research examines the dynamics of vitamin E entry and exit in proteins and its relationship with the control of blood vitamin E level in humans. Vitamin E is the most important lipophilic antioxidant and is involved in all aging diseases, such as heart diseases, cancer, and Alzheimer’s disease. Because vitamin E does not dissolve in water, vitamin E inside a cell is completely engulfed in the hydrophobic core of proteins. Thus, the entry and exit of vitamin E in those proteins have to involve protein motion.

Selected Publications:
F. Cordier, C. Wang, S. Grzesiek, and L.K. Nicholson, “Ligand-Induced Strain in Hydrogen Bonds of the c-Src SH3 Domain Detected by NMR,” Journal of Molecular Biology, 304, 497-505, (2000). Published with an accompanying cover illustration and highlighted on the Academic Press website.

C. Wang, J. Xi, T.P. Begley, and L.K. Nicholson, “Solution Structure of ThiS and Implications for the Evolutionary Roots of Ubiquitin,” Nature Structural Biology, 8, 47-51, (2001). Selected as Editor’s Choice in Jan 19, 2001 issue of Science.

C. Wang, N. Pawley, and L. Nicholson, “The Role of Backbone Motions in Ligand Binding to the c-Src SH3 Domain,” Journal of Molecular Biology, 313, 873-887, (2001).

C. Wang, M.J. Grey, and A.G. Palmer, “New CPMG Sequences with Enhanced Sensitivity to Chemical Exchange,” Journal of Biomolecular NMR, 21, 361-366, (2001).

C. Wang and A.G. Palmer, “Differential Multiple Quantum Relaxation Caused by Chemical Exchange outside Fast Exchange Limit,” Journal of Biomolecular NMR, 24, 263-268, (2002).

C. Wang, M. Rance, and A.G. Palmer, “Mapping Chemical Exchange in Proteins with MW 50 kD,” Journal of the American Chemical Society, 125, 8968-8969, (2003). Selected as a “Must Read” by www.facultyof1000.com.

C. Wang and A.G. Palmer, “Solution NMR Methods for Quantitative Identification of Chemical Exchange in 15N-labeled Proteins,” Magnetic Resonance in Chemistry, 41, 866-876, (2003).

M.J. Grey, C. Wang, and A.G. Palmer, “Disulfide Bond Isomerization in Basic Pancreatic Trypsin Inhibitor: Multi-Site Chemical Exchange Quantified by CPMG Relaxation Dispersion and Chemical Shift Modeling,” Journal of the American Chemical Society, 125, 14324-14335, (2003).

F. Massi, E. Johnson, C. Wang, M. Rance, and A.G. Palmer, “NMR T1p Rotating-frame Relaxation with Weak Radiofrequency Fields,” Journal of the American Chemical Society, 126, 2247-2256, (2003).

C. Wang, N.K. Karpowich, J.F. Hunt, M. Rance, and A.G. Palmer, “Dynamics of ATP-Binding Cassette Contribute to Allosteric Control, Nucleotide Binding and Energy Transduction in ABC Transporters,” Journal of Molecular Biology, in press, (2004).

Contact Information:
Chunyu Wang
No email or phone available yet.
http://j2ee.rpi.edu/biology/update.do?artcenterkey=59