Zengyi Chang, Ph.D.

Professor of Biochemistry and Molecular Biology
Associate Dean, School of Life Sciences, Peking University
Director, Center for Protein Science, Peking University

tel : 86 - 10 - 6275-8822

fax : 86 - 10 - 6275-1526

New Life Science Building, Peking University, Summer Palace Road No. 5, Beijing, P. R. China 100871

Research Interests

Interesting point of Chang Lab:

  1. Stress response and aging mechanism
  2. Mechanism and biological significance of protein-protein interactions

All living organisms unavoidably experience stress conditions like heat, extreme pH value, ROS attack, etc. Under such stress conditions, the structure of large molecules including DNA, RNA, and proteins that are maintained by non-covalent weak interaction are changed, among which conformation of protein probably is most severely affected. Unfolding of protein often leads to protein aggregation, which means the loss of biological function. Previous researches demonstrate that all organism genomes encode a kind of proteins named chaperone (heat shock protein or stress protein). Chaperone plays a key role in protecting proteins that are prone to unfolding or aggregation. These “guard” proteins play a role during the whole life time-- “birth, aging, sickness, and death” of their client proteins. The questions that we try to answer are：How stress proteins function to protect other proteins from unfolding or aggregation in vivo? How immediate conformational change of stress proteins responding to stress leads to sharp increase of their biological activity? What is the molecular mechanism of some organisms adopting dormancy to cope with extreme stresses? What is the molecular mechanism of aging?

Proteins function through interacting with other molecules. Proteins can form homo-oligomers or hetero-oligomers. Although previous in vivo and in vitro studies discovered a huge amount of specific interactions between proteins, transient or weak interactions in vivo remains to be identified and further investigated. In this field, the questions that we try to answer are: whether many proteins that are previously identified existing as monomers actually exist as homo-oligomers? How can we identify protein interaction partners in vivo? How do these homo-oligomers and hetero-oligomers fulfill their specific biological functions?

Lab page: http://www.bio.pku.edu.cn/lab/proteinsci/

Publications