Prof. Dr. Lichun He 

Wuhan Institute of Physics and Mathematics, CAS

Innovation Academy for Precision Measurement Science and Technology, CAS

University of Chinese Academy of Sciences

Lichun He was appointed as professor at the Wuhan Institute of Physics and Mathematics of the Chinese Academy of Sciences in 2019. His current research focuses on understanding structure, dynamics and function of biological systems by using nuclear magnetic resonance spectroscopy and other biophysical methods. He is also interested in NMR methods development.

Research Areas

1. Mechanism of Biologcial Molecules Explored via NMR spectroscopy in Solution and Its Native Enviorments

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. Mechanism of Bacteria Alter Host Innate Immune Response via Outer Membrane Vesicles(OMVs)

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. Mechanism of Transmembrane Domain in Signaling Transduction

We applied NMR to investigate the structural and functional roles of the transmembrane and membrane-proximal regions of cell surface proteins with special focus on CAR-T transmembrane domain, innate immune response receptors and viral proteins.

4. Nanobody Screening and Epitope Mapping via NMR

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.


Editorship & Membership

2021-07, LIFE,  Special Issue Editor

2021-08, BIOMOLECULES,  Topical Advisory Panel Membership



      Yaling Zhao                  Yang Qiao 

      Technician                   Technician 


University of Basel, Switzerland

Friedrich-Loeffler-Institut, Germany

Graduate Student


   Gangjin Yu          Guan Wang         Yihao Chen          Saba Bashir         Yicong Liu         Zhiqing Tao       Mingjun Zhu

       Postdoc.             Graudate Student      Graudate Student       Graudate Student     Graudate Student    Graudate Student    Graudate Student


ChaoZhe Wang       Huan Wang

 Graudate Student       Graudate Student 

Undergraduate Student

Zhuoyue Jinyang



(1) Cellular stress promotes NOD1/2-dependent inflammation via the endogenous metabolite sphingosine-1-phosphate, The EMBO Journal, 2021

(2) NMR-Based Methods for Protein Analysis, Anal Chem., 2020

(3) Mechanisms of Chaperones as Active Assistant/Protector for Proteins: Insights from NMR Studies, Chinese Journal of Chemistry, 2019-12

(4) Frustrated Interfaces Facilitate Dynamic Interactions between Native Client Proteins and Holdase Chaperones, ChembioChem, 2019-06

(5) Common Patterns in Chaperone Interactions with a Native Client Protein., Angew.Chemie Int. Ed., 2018,

(6) An unexpected protective role of low affinity allergen-specific IgG via the inhibitory receptor FcrRIIb, J. Allergy Clin. Immunol., 2017, 

(7) Therapeutic silence of pleiotrophin by targeted delivery of siRNA and its effect on the inhibition of tumor growth and metastasis, PLoS One, 2017

(8) A molecular mechanism of chaperone-client recognition., Science Advances, 2016

(9) Structure determination of helical filaments by solid-state NMR spectroscopy, Proc Natl Acad Sci U S A., 2016

(10) Solid-state NMR resonance assignments of the filament-forming CARD domain of the innate immunity signaling protein MAVS, Biomol NMR Assign., 2014

(11) Expression, purification, refolding, and characterization of octreotide-interleukin-2: a chimeric tumor-targeting protein, Int J Mol Med., 2011



Prof. Dr. Lichun He 

Wuhan Institute of Physics and Mathematics, CAS

Add:West No.30 Xiao Hong Shan,Wuhan 430071 China


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