• Bulletin of the Korean Chemical Society
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• v.24 no.7
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• pp.899-900
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• 2003

• Journal of the Korean Society for Precision Engineering
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• v.17 no.11
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• pp.88-93
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• 2000

Recently the gear design focuses on the optimal design to extract the design factors from the vehicle transmission that is required to equip the powerful, speedy and silent characteristics. In this study, we had determined modules($m_n$) and face widths (b) to sustain strengths of contact and bending. The pressure angle ($\alpha$) and the helix angle ($\beta$) also had been obtained from the constraint of a contact ratio ($\varepsilon) on helical gears. Through the optimal design algorithm suggested in this study, the design factors were calculated on vehicle transmission gears and those determined factors were able to firm a suitability of the design.

• Molecules and Cells
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• v.44 no.3
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• pp.179-185
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• 2021

Vancomycin response regulator (VncR) is a pneumococcal response regulator of the VncRS two-component signal transduction system (TCS) of Streptococcus pneumoniae. VncRS regulates bacterial autolysis and vancomycin resistance. VncR contains two different functional domains, the N-terminal receiver domain and C-terminal effector domain. Here, we investigated VncR C-terminal DNA binding domain (VncRc) structure using a crystallization approach. Crystallization was performed using the micro-batch method. The crystals diffracted to a 1.964 Å resolution and belonged to space group P212121. The crystal unit-cell parameters were a = 25.71 Å, b = 52.97 Å, and c = 60.61 Å. The structure of VncRc had a helix-turn-helix motif highly similar to the response regulator PhoB of Escherichia coli. In isothermal titration calorimetry and size exclusion chromatography results, VncR formed a complex with VncS, a sensor histidine kinase of pneumococcal TCS. Determination of VncR structure will provide insight into the mechanism by how VncR binds to target genes.

• BMB Reports
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• v.32 no.3
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• pp.279-287
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• 1999

The aromatic hydrocarbon receptor (AhR) is a cytosolic protein that binds the environmental pollutant, dioxin. The liganded AhR translocates into the nucleus where it heterimerizes with a constitutive nuclear protein, AhR nuclear translocator (Arnt). The N-terminal regions of both AhR and Arnt contain basic helix-loop-helix (bHLH) and Per-AhR-Arnt-Sim (PAS) motifs that are required for DNA binding, dimerization, and ligand binding whereas the C-terminal regions of both AhR and Arnt contain transactivation domains. Here, results from the mammalian two-hybrid system indicate that Arnt can make a homodimer but AhR cannot. In the presence of dioxin, the interaction between AhR and Arnt is stronger than that of the Arnt homodimer, suggesting that Arnt prefers to make a heterodimer with the liganded AhR rather than a homodimer. Transfection analyses using the GAL4-driven reporter system suggest that AhR's N-terminal region represses its own transactivation domain, as well as exogenous transactivation domains such as Sp 1 and VP16. Interestingly, the repressed transactivation domains of AhR are activated by ligand-dependent heterodimerization with Arnt. These observations suggest that heterodimerzation with Arnt is necessary not only for DNA binding but also for activation of the repressed transactivation capability of AhR.

• The Korean Journal of Malacology
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• v.24 no.1
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• pp.73-80
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• 2008

Numerous morphological studies on N. samarangae have been well conducted over the last ten years. In this context, we have attemtped to do molecular phylogenetic analysis by using metallothionein (MT) gene from N. samarangae. To this end, we cloned the full length cDNA of MT from cDNA library of N. samarangae. The complete cDNA sequences were obtained from the expressed sequence tag (EST) sequencing project of N. samarangae, The coding region of 195 bp gives an amino acid sequence of 65 residues including methionine. There are 5' (61 bp) and 3' (48 bp) untranslated region at both ends of the Ns-MT cDNA sequence. The combined results from BLAST analyses, multiple sequence alignment and molecular phylogenetic study of Ns-MT cDNA indicate that N. samarangae has similarity to land snails such as Helix pomatia, Helix aspersa and Arianta arbustorum.

• BMB Reports
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• v.40 no.5
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• pp.740-748
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• 2007

To gain insight into the structure and function of repressor proteins of bacteriophages of gram-positive bacteria, repressor of temperate Staphylococcus aureus phage ${\phi}11$ was undertaken as a model system here and purified as an N-terminal histidine-tagged variant (His-CI) by affinity chromatography. A ~19 kDa protein copurified with intact His-CI (~ 30 kDa) at low level was resulted most possibly due to partial cleavage at its Ala-Gly site. At ~10 nM and higher concentrations, His-CI forms significant amount of dimers in solution. There are two repressor binding sites in ${\phi}11$ cI-cro intergenic region and binding to two sites occurs possibly by a cooperative manner. Two sites dissected by HincII digestion were designated operators $O_L$ and $O_R$, respectively. Equilibrium binding studies indicate that His-CI binds to $O_R$ with a little more strongly than $O_L$ and binding species is probably dimeric in nature. Interestingly His-CI binding affinity reduces drastically at elevated temperatures ($32-42^{\circ}C$). Both $O_L$ and $O_R$ harbor a nearly identical inverted repeat and studies show that ${\phi}11$ repressor binds to each repeat efficiently. Additional analyses indicate that ${\phi}11$ repressor, like $\lambda$ repressor, harbors an N-terminal domain and a C-terminal domain which are separated by a hinge region. Secondary structure of ${\phi}11$ CI even nearly resembles to that of $\lambda$ phage repressor though they differ at sequence level. The putative N-terminal HTH (helix-turn-helix) motif of ${\phi}11$ repressor belongs to the HTH -XRE-family of proteins and shows significant identity to the HTH motifs of some proteins of evolutionary distant organisms but not to HTH motifs of most S. aureus phage repressors.

• Aerospace Engineering and Technology
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• v.13 no.1
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• pp.10-19
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• 2014

We designed bearingless rotor hub system which replace mechanical hinge/bearing with composite beam component and conducted fatigue analysis for flexbeam and torque tube. Extension/bending/torsional stiffness was calculated from 2D section analysis using VABS and 2D section structure analysis was applied for strain calculation. S-N curve of each composite material was generated using Wohler equation and fatigue analysis was conducted on weakness section which was decided from static structure analysis. CAMRAD II was used for load analysis and load analysis result was applied HELIX/FELIX standard load spectrum to generate bearingless rotor system load spectrum which was used fatigue safe life analysis.

• Journal of Veterinary Science
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• v.21 no.4
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• pp.52.1-52.11
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• 2020

Background: Intradural-intramedullary intervertebral disc extrusion (IIVDE) is a rare condition of intervertebral disc disease. However, the diagnosis of IIVDE is challenging because the prognosis and imaging characteristics are poorly characterized. Objectives: We aimed to describe the clinical and imaging characteristics of tentatively diagnosed IIVDE in dogs to assess the prognostic utility of neurological grade and magnetic resonance imaging (MRI) findings. Methods: Twenty dogs were included in this retrospective cohort study. Results: Nonchondrodystrophic breeds (n = 16) were more predisposed than chondrodystrophic breeds. Most dogs showed acute onset of clinical signs. Neurological examination at admission showed predominant non-ambulatory paraparesis (n = 9); paresis (n = 16) was confirmed more frequently than paralysis (n = 4). Follow-up neurological examination results were only available for 11 dogs, ten of whom showed neurological improvement and 8 showed successful outcomes at 1 month. The characteristic MRI findings include thoracic vertebra (T)2 hyperintense, T1 hypointense, intramedullary linear tracts with reduced disc volume, and cleft of the annulus fibrosus. None of the MRI measurements were significantly correlated with neurological grade at admission. Neurological grade did not differ according to the presence of parenchymal hemorrhage, parenchymal contrast enhancement, and meningeal contrast enhancement. Neurological grades at admission showed a statistical correlation with those observed at the 1-month follow-up (r = 0.814, p = 0.02). Conclusions: IIVDE is a rare form of disc extrusion commonly experienced after physical activity or trauma and most frequently affects the cranial-cervical and thoracolumbar regions of nonchondrodystrophic dog breeds. Neurological score at admission emerged as a more useful prognostic indicator than MRI findings in dogs with suspected IIVDE.

• Journal of the Korean Chemical Society
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• v.38 no.10
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• pp.710-718
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• 1994

We suggest a statistical thermodynamic theory for the conformational transition of a synthetic alanine (Ala), ${\alpha}$-aminoisobutyric acid (Aib) alternative oligopeptide, Buo-(Ala-Aib)$_n$-oMe, where the terminal groups Buo and oMe stand for t-butoxy and methoxy, respectively. Pure Aib homo-oligomers have always been found to adopt $3_{10}$ helical conformations, while polyalanine has always $\alpha$ helical conformation. In an organic solvent (e.g. $CD_3$CN) it shows that the length for the $3_{10}$/${\alpha}$ helix transitions of Buo-(Ala-Aib)$_n$-oMe, is 8 at room temperature. In an aqueous solution oligopeptide has always coil conformation at room temperature. In an organic solution, helical structures of the oligopeptide are more stable than coil structure, so we studied the $$3_{10}/\alpha$ helix transitions, considering coiled-conformations, coiled and $3_{10}$ helical conformations, and coiled and $\alpha$ helical conformations by using the zipper model. We determined the values of parameters ($\sigma_A$, $\sigma_T$, $\xi_A$, $\xi_T$) from the relating published data; $\sigma_A$ = 0.00011, $\sigma_T$ = 0.0060, $\xi_A$ = 10.1, $\xi_T$ = 3.90. The distributions of $\alpha$ helical length can be N-2, N-3, N-4, ${\cdots}$, 3, 2, 1 (N = 2n) while those of $3_{10}$ helical length, N-1, N-2, N-3, N-4, ${\cdots}$, 3, 2, 1.

• Journal of the Korean Chemical Society
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• v.67 no.2
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• pp.81-88
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• 2023

The contribution of hydrophobic residues to the protein folding reaction was studied by using HubWA variant proteins with I and L to V mutation. Folding kinetics of all V variant proteins was observed to be satisfied by a three-state on-pathway mechanism, U ⇌ I ⇌ N, where U, I, and N represent unfolded, intermediate, and native state, respectively. Three-state folding reaction was quantitatively analyzed and the free energy of folding of each elementary reactions and overall folding reaction, ΔG^o_UI, ΔG^o_IN, and ΔG^o_UN, were obtained. From the ratio of free energy difference between the variant protein and HubWA, ΔΔG^o_UI/ΔΔG^o_UN (ΔΔG^o_UI = ΔG^o_UI (variant protein) - ΔG^o_UI (HubWA) and ΔΔG^o_UN = ΔG^o_UN (variant protein) - ΔG^o_UN(HubWA)), the contribution of hydrophobic residues to HubWA folding was analyzed. The residues which are located in the hydrophobic core between α-helix and β-sheet, I3, I13, L15, I30, L43, I61 and L67, showed ΔΔG^o_UI/ΔΔG^o_UN value of ~0.5 when each of these residues was mutated to V, indicating that these residues form relatively solid hydrophobic core in the intermediate state. Residues located at the end of secondary structures and loop, I23, L69 and I36 showed ΔΔG^o_UI/ΔΔG^o_UN value below 0.4 when each of these residues was mutated to V, indicating that the region containing these residues are loosely formed in the intermediate state. V17A, L50V and L56V showed fairly high ΔΔG^o_UI/ΔΔG^o_UN value of ~0.8. Since L50 and L56 are located in the region containing long loop (residue 46 to 62), it is suggested that the high ΔΔG^o_UI/ΔΔG^o_UN value of these residues prevents the formation of aggregate at the early stage of folding reaction.