Pohang University of Science and Technology · 材料科学
Professor Kyeong Sik Jin's research lab specializes in the structural characterization of biomolecules in solution using advanced biophysical techniques, particularly synchrotron small-angle X-ray scattering (SAXS), circular dichroism, and Raman spectroscopy. The lab focuses on understanding the conformational dynamics and structural transitions of nucleic acids (such as i-motif DNA and duplex DNA) and proteins (including pepsin and transcriptional regulators) under varying environmental conditions like pH, denaturants, and ligand binding. A central theme is the investigation of structural flexibility, folding, and functional modulation in biological macromolecules, with an emphasis on dynamic and disordered states that are often overlooked in traditional crystallographic studies. The lab also explores the effects of nanomaterials, such as fullerenes, on DNA structure and stability, highlighting interdisciplinary approaches at the interface of biophysics, structural biology, and nanoscience.
Figures are computed from collected data and may differ slightly.
The pH-dependent structures of the ferritin shell (apoferritin, 24-mer) and the ferrihydrite core, under physiological conditions that permit enzymatic activity, were investigated by synchrotron small-angle X-ray scattering (SAXS). The solution structure of apoferritin was found to be nearly identical to the crystal structure. The shell thickness and hollow core volumes were estimated. The intact hollow spherical apoferritin was stable over a wide pH range, 3.40−10.0, and the ferrihydrite core w
The first in-situ two-dimensional grazing incidence small-angle X-ray scattering (2D GISAXS) study on the evolution of nanopores during the thin film formation of porous dielectrics from composite films is reported. A soluble poly(methylsilsesquioxane) (PMSSQ) precursor and a four-armed poly(E-caprolactone) (PCL4) were chosen as the model matrix and porogen components within the composite film. The measured 2D GISAXS data were analyzed quantitatively using a GISAXS formula derived under the dist
In order to achieve a hydrogel capable of programmable volume change, poly(N-isopropylacrylamide)-graft-methylcellulose hydrogel (PNIPAm-g-MC) was prepared through the grafting of PNIPAm onto a MC backbone and simultaneous cross-linking of the chains. PNIPAm-g-MC exhibited large thermal hysteresis in its volume change, which results from the stable hydrophobic junctions between the MC strands formed during heating. By combining photothermal magnetite nanoparticles as a heat transducer with the p
There are two beamlines (BLs), 4C1 and 4C2, at the Pohang Accelerator Laboratory that are dedicated to small angle X-ray scattering (SAXS). The 4C1 BL was constructed in early 2000 and is open to public users, including both domestic and foreign researchers. In 2003, construction of the second SAXS BL, 4C2, was complete and commissioning and user support were started. The 4C2 BL uses the same bending magnet as its light source as the 4C1 BL. The 4C1 BL uses a synthetic double multilayer monochro
We have investigated for the first time the structure of i-motif DNA in solution at various pH conditions by using synchrotron small-angle X-ray scattering technique. To facilitate direct structural comparison between solution structures of i-motif DNA at various pH values, we created atomic coordinates of i-motif DNA from a fully folded to unfolded atomic model. Under mild acidic conditions, the conformations for i-motif DNA appeared to be similar to that of the partially unfolded i-motif atomi
Katanin was the first microtubule (MT)-severing enzyme discovered, but how katanin executes MT severing remains poorly understood. Here, we report X-ray crystal structures of the apo and ATPγS-bound states of the catalytic AAA domain of human katanin p60 at 3.0 and 2.9 Å resolution, respectively. Comparison of the two structures reveals conformational changes induced by ATP binding and how such changes ensure hexamer stability. Moreover, we uncover structural details of pore loops (PLs) and show
The structural characteristics of aqueous micelles composed of amphiphilic cyclic poly(<i>n</i>-butyl acrylate-<i>b</i>-ethylene oxide) (cyclic PBA-<i>b</i>-PEO) or a linear analogue (i.e., linear poly(<i>n</i>-butyl acrylate-<i>b</i>-ethylene oxide-<i>b</i>-<i>n</i>-butyl acrylate) (linear PBA-<i>b</i>-PEO-<i>b</i>-PBA)) were examined for the first time using synchrotron X-ray scattering techniques and quantitative data analysis. The scattering data were analyzed using a variety of methodologie
In higher eukaryotes, one of the two arginyl-tRNA synthetases (ArgRSs) has evolved to have an extended N-terminal domain that plays a crucial role in protein synthesis and cell growth and in integration into the multisynthetase complex (MSC). Here, we report a crystal structure of the MSC subcomplex comprising ArgRS, glutaminyl-tRNA synthetase (GlnRS), and the auxiliary factor aminoacyl tRNA synthetase complex-interacting multifunctional protein 1 (AIMP1)/p43. In this complex, the N-terminal dom
Structural characteristics of various conformational states of porcine pepsin in solution under different pH conditions were investigated in terms of size and shape by small-angle X-ray scattering (SAXS). Low-resolution structural models of porcine pepsin were reconstructed from SAXS data, which were made inside the search volume of maximum dimension (Dmax), calculated from the pair distance distribution function p(r). The reconstructed structural models were obtained without imposing any restri
The structural effects of fullerene on i-motif DNA were investigated by characterizing the structures of fullerene-free and fullerene-bound i-motif DNA, in the presence of cDNA and in solutions of varying pH, using circular dichroism and synchrotron small-angle X-ray scattering. To facilitate a direct structural comparison between the i-motif and duplex structures in response to pH stimulus, we developed atomic scale structural models for the duplex and i-motif DNA structures, and for the C(60)/
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