主要研究方向：

1. 核磁共振波谱技术研究蛋白质（如分子伴侣等）激发态、蛋白质动力学性质及其介导的动态相互作用

Chaperones are crucial for cellular life to ensure all proteins obtain their right fold and functionality. The promiscuous property of chaperones enables them to bind with a wide spectrum of client proteins from nascent proteins to quasi-native and native proteins. While mechanisms of chaperones aided protein folding have been intensively characterized, it is still largely unknown how chaperones act on folded clients and modulate the activity of the folded protein. To address this fundamental question, We apply NMR spectroscopy and other biophysics approaches to understand chaperone and client proteins recognition and interaction by investigating their intermediate conformations (excited state), protein dynamics modulations and the subsequently changes of its activities. 

2. 利用细菌外分泌囊泡为建立细菌感染与机体免疫反应的NMR研究体系

Bacterial outer membrane vesicles (OMVs) are nano‐sized compartments consisting of a lipid bilayer that encapsulates periplasm‐derived, luminal content. OMVs, which pinch off of Gram‐negative bacteria, are now recognized as a generalized secretion pathway which provides a means to transfer cargo to other bacterial cells as well as eukaryotic cells. Although it is well recognized that OMVs can enter and release cargo inside host cells during infection, the mechanisms of host association and uptake are not well understood. We apply biophysical, biochemical and cellular biological approaches to investigate characters of virulence factors in OMVs and study the mechanism of host cell association, uptake and innate immunue response to OMVs.

3. 纳米抗体筛选及利用NMR对抗原结合表位的表征

Single-domain antibody, also known as a nanobody, is an antibody fragment from Camelid consisting of a single monomeric variable antibody domain. It has a molecular weight of only 12–15 kDa. Nevertheless it is able to bind with a particular antigen with a high affinity. Besides higher affinity, smaller size, nanobody also has other advantages such as higher stability and easy expression in E.coli facilitating isotope labeling and epitope mapping via NMR.