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Research Interests
My research (Current Research Scope) involves single-molecule spectroscopy studies of molecular kinetics and dynamics in condensed phase and at interfaces. Research on the single-molecule/nanoparticle interfacial electron transfer dynamics represents an applications of single-molecule approaches to study an important interfacial chemical reaction that was traditionally studied by ensemble-averaged experiments. We have been applying single-molecule fluorescence and surface-enhanced Raman spectroscopies to obtain detailed Franck-Condon vibronic coupling, electron-transfer driving forces, and solvent relaxation energies of electron donor molecules and the nanoparticles. In the area of reaction and dynamics in proteins and protein complexes, we are studying the dynamics and mechanisms of single-molecule enzymatic reactions and non-covalent DNA-protein and protein-protein interactions. Non-Arrhenius and non-Markovian dynamics, allosteric effect, cooperativity, and memory effects of enzymatic reactions have been widely observed but are poorly understood due to the nature of the static and dynamic inhomogeneities in an ensemble-averaged measurement as well as in the intrinsic molecular dynamics. By applying single-molecule approaches, we have been able to investigate the protein conformational relaxation and fluctuation behaviors to identify the protein conformational motion dynamics and the correlated enzymatic turnover dynamics and mechanisms. Our research has also provided unique experimental identifications and characterizations of fluctuating noncovalent protein-protein interactions in cell signaling and protein-DNA interactions in DNA damage recognition. These fluctuating and inhomogeneous conformational motions in protein-protein and protein-DNA complexes most likely determine the capability of protein recognitions and DNA damage recognition. We also developed a number of AFM-tip enhanced NSOM fluorescence and Raman optical imaging approaches that are capable of obtaining Raman or fluorescence imaging beyond optical diffraction limited spatial resolution. We had applied our AFM-tip enhanced or correlated optical imaging approaches to analyzing bacterial cell membrane proteins.
Single-Molecule Conformational Dynamics of Protein-Protein Interactions in Cell Signaling
Single-Molecule Ion Channel Conformational Dynamics
Single-Molecule Dynamics of Protein-DNA Interactions in DNA Damage Recognition
Site-specific and single-molecule spectroscopy studies on inhomogeneous interfacial electron transfer dynamics
Developments of state-of-the-art single-molecule temporal and spatial spectroscopy capabilities for studying protein conformational dynamics and enzymatic reaction dynamics
My research (Current Research Scope) involves single-molecule spectroscopy studies of molecular kinetics and dynamics in condensed phase and at interfaces. Research on the single-molecule/nanoparticle interfacial electron transfer dynamics represents an applications of single-molecule approaches to study an important interfacial chemical reaction that was traditionally studied by ensemble-averaged experiments. We have been applying single-molecule fluorescence and surface-enhanced Raman spectroscopies to obtain detailed Franck-Condon vibronic coupling, electron-transfer driving forces, and solvent relaxation energies of electron donor molecules and the nanoparticles. In the area of reaction and dynamics in proteins and protein complexes, we are studying the dynamics and mechanisms of single-molecule enzymatic reactions and non-covalent DNA-protein and protein-protein interactions. Non-Arrhenius and non-Markovian dynamics, allosteric effect, cooperativity, and memory effects of enzymatic reactions have been widely observed but are poorly understood due to the nature of the static and dynamic inhomogeneities in an ensemble-averaged measurement as well as in the intrinsic molecular dynamics. By applying single-molecule approaches, we have been able to investigate the protein conformational relaxation and fluctuation behaviors to identify the protein conformational motion dynamics and the correlated enzymatic turnover dynamics and mechanisms. Our research has also provided unique experimental identifications and characterizations of fluctuating noncovalent protein-protein interactions in cell signaling and protein-DNA interactions in DNA damage recognition. These fluctuating and inhomogeneous conformational motions in protein-protein and protein-DNA complexes most likely determine the capability of protein recognitions and DNA damage recognition. We also developed a number of AFM-tip enhanced NSOM fluorescence and Raman optical imaging approaches that are capable of obtaining Raman or fluorescence imaging beyond optical diffraction limited spatial resolution. We had applied our AFM-tip enhanced or correlated optical imaging approaches to analyzing bacterial cell membrane proteins.
Single-Molecule Conformational Dynamics of Protein-Protein Interactions in Cell Signaling
Single-Molecule Ion Channel Conformational Dynamics
Single-Molecule Dynamics of Protein-DNA Interactions in DNA Damage Recognition
Site-specific and single-molecule spectroscopy studies on inhomogeneous interfacial electron transfer dynamics
Developments of state-of-the-art single-molecule temporal and spatial spectroscopy capabilities for studying protein conformational dynamics and enzymatic reaction dynamics
Research Interests
Papers共 545 篇Author StatisticsCo-AuthorSimilar Experts
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CHEMICAL PHYSICS IMPACT (2022): 100060
JOURNAL OF CHEMICAL PHYSICSno. 5 (2022): 055102
Cancer management and research (2021): 2371-2378
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Author Statistics
#Papers: 540
#Citation: 21862
H-Index: 70
G-Index: 132
Sociability: 7
Diversity: 4
Activity: 45
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