Kyung Hee University · 生化学・遺伝学・分子生物学
Professor Seong Ho Kang's research lab specializes in advanced analytical methodologies at the intersection of biophysics, nanomaterials, and bioimaging. The lab focuses on single-molecule fluorescence imaging, particularly using evanescent field microscopy and total internal reflection fluorescence (TIRF) to study the conformational dynamics and surface interactions of biomolecules such as DNA and proteins. Key research directions include the development of novel photochromic probes for live-cell imaging, multimodal capillary electrophoresis for high-throughput peptide mapping, and metal-enhanced fluorescence (MEF) for ultrasensitive biosensing. The lab also pioneers microchip-based capillary electrophoresis for rapid, miniaturized analysis of genomic and proteomic samples, with applications in biotechnology and food safety.
Figures are computed from collected data and may differ slightly.
The conformational dynamics and adsorption/desorption behavior of individual lambda-DNA molecules at liquid-solid interfaces were monitored by imaging within the evanescent field layer using total internal reflection fluorescence microscopy. At a fused-silica surface, molecular conformation and adsorption behavior were found to depend on both pH and buffer composition. A histogram of individual lambda-DNA adsorption durations measured by hydrodynamically flowing molecules along the interface exh
A new diarylethene-derived photochromic compound, with little cytotoxicity, plasma membrane-permeability, and efficient photoswitchability in cells upon alternative UV and visible light irradiation, was synthesized and applied to live cell imaging.
The behavior of individual molecules of R-phycoerythrin (RPE) was monitored by fluorescence imaging at various pHs and ionic strengths within the evanescent-field layer (EFL) at a water/fused-silica interface. Above the isoelectric point (pI), the individual protein molecules moved between exposures with random motion. As the pH approached the pI of the protein, the RPE molecules were partially adsorbed onto the fused-silica surface. The residence time and the number of molecules within the EFL
A novel multimodal method for peptide mapping of proteins by multiplexed capillary electrophoresis (CE) is presented. By combining charge to size separations in four different channels and micellar electrokinetic chromatography for hydrophobicity-based separations in two different channels in a 96-capillary array, peptide fragments of digested proteins were readily resolved and showed unique fingerprints. Each capillary spanned several diodes in a photodiode array (PDA) for absorption measuremen
Abstract Microchip‐based capillary electrophoresis (ME) raises fascinating possibilities for new analytical technologies particularly in the detection of DNA fragments in modern biology. The ME technique has gained considerable popularity with significant progress being made in the development of miniaturized microfluidic devices in micro‐volume analysis methods. The ME offers the potential for highly efficient, simultaneous analysis of a large number of biologically important molecules in genom
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