OUR RESEARCH
Our research interests focus on probing the structure and dynamics of biomolecules, nano-bio complex materials, and their interactions with water through neutron and X-ray scattering spectroscopy and theoretical modeling. We are attempting to reveal the underneath mystery of bio-macromolecules, especially protein, DNA and RNAs. This will help us understand how their functions and dynamics are driven and how they affect our lives.
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Enzymatic catalysis and Quantum Tunneling effect:
It is generally believed that the biological function and activities of proteins are intimately related to their structures and dynamics. The purpose of this project is to provide solid and quantitative evidence for the connections between the dynamics of enzymes and their biological activity and to further explore possible quantum tunneling effects, or hydrogen tunneling in enzymatic catalysis.
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Phonons in native and denatured proteins:
Detecting phonons in native and denatured proteins is essential for understanding the intra-protein dynamical behavior. The aim of this research is to obtain a full map of the milli-eV phonon-like excitations in the fully deuterated protein.
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Assembly mechanisms of Reflectins for cephalopods’ camouflage
Reflectins are unique proteins existing in cephalopods that can quickly change the color of their skin, to achieve the purpose of camouflage and communication. In this project, we are trying to understand the assembly mechanisms of reflectins and their interactions with lipids and membranes from all aspects by various neutron and X-ray scattering. Currently, we are collaborating with the Songshan Lake Deuteration Facility (SLDF) at the Songshan Lake Materials Laboratory on this project.
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Dynamic Behavior of Proteins under Extreme Conditions:
We are trying to understand the relationships between the slow dynamics of protein molecules and its functions by studying proteins under extreme conditions, such as high pressure, and extremely low and high temperatures. Proteins from hyperthermophilic (heat-loving) and barophilic (high-pressure) organisms are the primary targets for this study.
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The fundamental mechanism of how antifreeze proteins prevent ice formation
Antifreeze glycoproteins (AFGPs) are an important biological complex and a novel set of proteins that can prohibit the formation of ice. Understanding prohibiting the crystallization of ice, synthesizing new cryoprotectants for conservation of tissues, cells, and food storage.
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Structural changes and dynamical basis of a G protein-coupled receptor (GPCR):
The structural changes and dynamical basis of a G protein-coupled receptor (GPCR) rhodopsin lead to the activation of the photoreceptor, which is responsible for triggering an amplified visual response in the process of vision.
