WANG ZHIZHEN Wang Zhizhen (Chihhen) is a biochemist. She was born in 1942 in Shanghai but is a native of Suzhou, Jiangsu Province. She obtained her Bs degree in biophysics in 1964 from the Department of Biophysics, University of Science and Technology of China. Since then on she has been working in the Institute of Biophysics, Chinese Academy of Sciences. She is currently a professor and the chairmen of the Academic Committee of the National Laboratory of Biomacromolecules. She was elected the academician of the Chinese Academy of Sciences in 2001, and the Fellow of the Third World Academy of Sciences in 2005. She carried researches also in laboratories in Germany, UK, USA, Canada, and Hong Kong. During 1995-2001 she was the Chinese Delegate to the Federation of Asian Oceanian Biochemists and Molecular Biologists. She joined the study on the interactions of A and B chains of insulin in her early time. Since 1993 she has concentrated on the macromolecules assisting protein folding—chaperones and foldases. She put forward a hypothesis of “Protein disulfide isomerase is both an enzyme and a chaperone” collaborating with Prof. C. L. Tsou, although this enzyme was previously believed to be an isomerase only and not a chaperone. She and her students demonstrated the intrinsic chaperone activity of the enzyme and the cooperative function of the two activities in catalyzing the folding of disulfidecontaining proteins. This new concept has now been accepted widely. They further characterized chaperone activity of bacteria thiolprotein oxidoreductase DsbC, which has been recognized as the first periplasmic protein possessing chaperone activity. The structures responsible for the two activities of protein disulfide isomerase, DsbC and chaperone DnaJ have been characterized. They provided evidence that dimerization creates chaperone and isomerase activity for monomeric thiolprotein oxidases or reductases. A new working mode for thiolprotein oxidoreductasesd has been proposed according to the above results.  In addition, her group characterized a short lived burstphase folding intermediate and captured a stable cold folding intermediate of Dglyceraldehyde3phosphate dehydrogenase, and revealed different binding modes of the chaperon GroEL with protein folding intermediate: “half of the site” and “all of the sites.” Wang Zhizhen has published more than 100 research and review papers, most of those in international journals, including EMBO J., Trends Biochem. Sci., FASEB J, PNAS, J. Biol. Chem., Biochemistry, Methods Enzymol., etc. She was invited to deliver more than 40 lectures at international conferences and in laboratories abroad. She has received several awards, including the National Natural Science Award (second class), the Third World Academy of Sciences Prize in Biology for 2002, the Natural Science Award of the Chinese Academy of Sciences (first and second class), and the title of “Young and middle aged expert with distinguished contributions to China.”