• BMB Reports
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• 제37권5호
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• pp.586-596
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• 2004

The folding of ervatamin C was investigated in the presence of various fluorinated and non-fluorinated organic solvents. The differences in the unfolding of the protein in the presence of various organic solvents and the stabilities of O-states were interpreted. At pH 2.0, non-fluorinated alkyl alcohols induced a switch from the native $\alpha$-helix to a $\beta$-sheet, contrary to the $\beta$-sheet to $\alpha$-helix conversion observed for many proteins. The magnitude of ellipticity at 215 nm, used as a measure of $\beta$-content, was found to be dependent on the concentration of the alcohol. Under similar conditions of pH, fluorinated alcohol enhanced the intrinsic a-helicity of the protein molecule, whereas the addition of acetonitrile reduced the helical content. Ervatamin C exhibited high stability towards GuHCl induced unfolding in different O-states. Whereas the thermal unfolding of O-states was non-cooperative, contrary to the cooperativity seen in the absence of the organic solvents under similar conditions. Moreover, the differential scanning calorimetry endotherms of the protein acquired at pH 2.0 were deconvoluted into two distinct peaks, suggesting two cooperative transitions. With increase in pH, the shape of the thermogram changed markedly to exhibit a major and a minor transition. The appearance of two distinct peaks in the DSC together with the non-cooperative thermal transition of the protein in O-states indicates that the molecular structure of ervatamin C consists of two domains with different stabilities.

• EDISON SW 활용 경진대회 논문집
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• 제4회(2015년)
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• pp.14-23
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• 2015

Alzheimer's disease is one of the most common types of degenerative dementia. As a considerable cause of Alzheimer's disease, neurotoxic plaques composed of 39 to 42 residue-long amyloid beta($A{\beta}$) fibrils have been found in the patient's brain in large quantity. A previous study found that erythrosine B (ER), a red color food dye approved by FDA, inhibits the formation of amyloid beta fibril structures. Here, in an attempt to elucidate the inhibition mechanism, we performed molecular dynamics simulations to demonstrate the conformational change of $A{\beta}40$ induced by 2 ERs in atomistic detail. During the simulation, the ERs bound to the surfaces of both N-terminus and C-terminus regions of $A{\beta}40$ rapidly. The observed stacking of the ERs and the aromatic side chains near the N-terminus region suggests a possible inhibition mechanism in which disturbing the inter-chain stacking of PHEs destabilizes beta-sheet enriched in amyloid beta fibrils. The bound ERs block water molecules and thereby help stabilizing alpha helical structure at the main chain of C-terminus and interrupt the formation of the salt-bridge ASP23-LYS28 at the same time. Our findings can help better understanding of the current and upcoming treatment studies for Alzheimer's disease by suggesting inhibition mechanism of ER on the conformational transition of $A{\beta}40$ at the molecular level.

• Molecules and Cells
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• 제39권6호
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• pp.495-500
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• 2016

We have solved the crystal structure of a predicted fructose-specific enzyme $IIB^{fruc}$ from Escherichia coli ($EcEIIB^{fruc}$) involved in the phosphoenolpyruvate-carbohydrate phosphotransferase system transferring carbohydrates across the cytoplasmic membrane. $EcEIIB^{fruc}$ belongs to a sequence family with more than 5,000 sequence homologues with 25-99% amino-acid sequence identity. It reveals a conventional Rossmann-like ${\alpha}-{\beta}-{\alpha}$ sandwich fold with a unique ${\beta}$-sheet topology. Its C-terminus is longer than its closest relatives and forms an additional ${\beta}$-strand whereas the shorter C-terminus is random coil in the relatives. Interestingly, its core structure is similar to that of enzyme $IIB^{cellobiose}$ from E. coli ($EcIIB^{cel}$) transferring a phosphate moiety. In the active site of the closest $EcEIIB^{fruc}$ homologues, a unique motif CXXGXAHT comprising a P-loop like architecture including a histidine residue is found. The conserved cysteine on this loop may be deprotonated to act as a nucleophile similar to that of $EcIIB^{cel}$. The conserved histidine residue is presumed to bind the negatively charged phosphate. Therefore, we propose that the catalytic mechanism of $EcEIIB^{fruc}$ is similar to that of $EcIIB^{cel}$ transferring phosphoryl moiety to a specific carbohydrate.

• International Journal of Industrial Entomology and Biomaterials
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• 제15권2호
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• pp.171-174
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• 2007

Sericin beads were prepared from ethanol-precipitated sericin. The addition of ethanol into hot-water extracted sericin solution induced precipitation of sericin and thereby some sericin could be fractionated. The ethanol-precipitated sericin (EpSS) had narrower molecular weight distribution than original sericin. The EpSS had mainly random coil structure with small portion of ${\beta}-sheet$ structure. With the EpSS, spherical beads could be prepared at lower concentration than with original sericin due to higher viscosity. The EpSS beads had better compressive strength than the original sericin beads and had rubber-like property. Our results suggest that EpSS is more compatible in the polymeric field, since it has better mechanical strength than original sericin.

• International Journal of Industrial Entomology and Biomaterials
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• 제25권1호
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• pp.133-137
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• 2012

To increase the solubility of lyophilized sericin, we added three types of lyoprotectant: sucrose, trehalose and dextran. The addition of lyoprotectant increased the solubility of lyophilized sericin especially when 1.0% of sucrose, 1.0% and 1.5% trehalose are added. The secondary structure of lyophilized sericin showed that the content of ${\beta}$-sheet or aggregated structure reduced in the presence of lyoprotectant. The morphology of lyophilized was also affected by the addition of lyoprotectant. Whereas flake structure was obtained in the case of pure sericin, a scattered and relatively small flake structure was formed in the presence of lyoprotectant. These finding shows that the presence of lyoprotectant prevents aggregation of sericin molecules and increases the solubility of lyophilized sericin.

• 한국잠사곤충학회지
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• 제52권1호
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• pp.10-15
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• 2014

작잠 누에고치를 정련한 후 질산칼슘4수화물의 용융액을 사용하여 재생 작잠 실크피브로인 스펀지를 제조하였다. 작잠 실크피브로인은 280 nm에서 tyrosine 잔기 등에 기인한 흡광대를 나타내었다. 작잠 실크피브로인 스펀지를 에탄올 농도별로 처리한 후 구조 전이를 관찰한 결과 80% 에탄올 처리시에는 ${\beta}$-sheet 구조($700cm^{-1}$), ${\alpha}$-helix 구조($625cm^{-1}$), 그리고 random coil ($660cm^{-1}$) 구조가 공존하는 것으로 나타났다. 또한 작잠 실크피브로인을 이용한 in vitro 상처회복실험 결과 실크피브로인의 첨가에 의하여 상처회복 효과가 인정되었다.

• 한국세라믹학회지
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• 제26권4호
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• pp.559-567
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• 1989

Bioglasses have been known to be as one of the promising biomateials, which can be used for replacing defective hard and soft tissue. There have been many reports on biological results for this type of glass, but no systematic work has carried out on the structures and properties of the bioglass itself. In the present study, the effect of P2O5 in bioglasses on their structures and properties was examined. Infrared and Raman spectroscopy for the glass structural analysis, differential thermal and X-ray diffraction analysis for the crystallization of the bioglass were performed, and several physical properties were measured. When the glasses were heat-treated, Na2O.2CaO.3SiO2 was the major crystalline phase and $\beta$-NaCaPO4 crystal was found for the glass with high P2O5 content. The added P2O5 in the glasses enhanced the polymerization of silicate glass structure and it changed the chain-like glass structure to a sheet-like structure, and some P2O5 may stay as phosphate monomer. With addition of P2O5 in the glass the density of the glasses decreased, but not much changes in their thermal expansion coefficient, softening point and microhardness were observed.

• 한국잠사곤충학회지
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• 제46권1호
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• pp.28-31
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• 2004

견피브로인의 응용가능성을 높이기 위하여 대표적인 생체고분자인 히아론산을 이용하여 견피브로인/히아론산 브렌드 필름을 제조하였으며 구조 및 열 특성을 살펴보았다. 1. 적외선 분광분석 결과 견피브로인과 히아론산 두 고분자 사이에는 수소결합 등의 상호작용이 존재하지 않는 것으로 나타났다. 또한 브렌드 필름내에 존재하는 실크피브로인은 EDC 에탄올 용액처리에 의하여 $\beta$-sheet 구조로 전이되었다. 2. 견피브로인/히아론산 브렌드 필름에서 견피브로인과 히아론산 각각의 열분해 흡열피크와 발열피크 온도에는 큰 변화가 없었으나, 열분해 피크의 폭이 넓어지는 것으로 봐서 실크 피브로인과의 브렌드 또는 EDC 처리에 의하여 열분해 반응이 매우 복잡한 환경하에서 진행되고 있음을 알 수 있었다. 3 견피브로인/히아로산 브렌드 필름은 자기 중량 대비 평균 70배의 수분을 흡수하였다.

• Archives of Pharmacal Research
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• 제15권1호
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• pp.52-57
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• 1992

The molecular structure of a natural compound was determined by single crystal X-ray diffraction analysis. The compound was isolated by methanol extraction and repeated chromatography from the stem of Paulownia tomentosa. Yellow prismatic crystals of the compound, which were recrystallized from tetrahydrofuran, are triclinic, with a = 7.310 (6), b = 10.753(6), c = 11.586(5) ${\AA}.\;\alpha= 93.30(6),\;\beta=105.62(10),\;\gamma=109.49(7)^\circ,\;D_x=1.514,\;D_m=1.51 g/cm^3$, space group P1 and Z = 2. The structure was solved by direct method, and refined by least-squares procedure to the final R-value of 0.032 for 1271 independent reflections $(F\le3\sigma{(F))}$. The compound is one of new furanquinone analogue. The molecule has a nearly planar conformation with an intramolecular hydrogen bond. In the crystal, the planar molecules are arranged as a prallel sheet-like pattern, and these stackings are stabilized by the O-H...O type intermolecular hydrogen bonds. The other intermolecular contacts appear to be the normal van der Waals interactions.

• BMB Reports
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• 제39권3호
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• pp.284-291
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• 2006

In this study, the cDNA of a new peptide from the venom of the scorpion, Buthotus saulcyi, was cloned and sequenced. It codes for a 64 residues peptide (Bsaul1) which shares high sequence similarity with depressant insect toxins of scorpions. The differences between them mainly appear in the loop1 which connects the $\beta$-strand1 to the $\alpha$-helix and seems to be functionally important in long chain scorpion neurotoxins. This loop is three amino acids longer in Bsaul1 compared to other depressant toxins. A comparative amino acid sequence analysis done on Bsaul1 and some of $\alpha$-, $\beta$-, excitatory and depressant toxins of scorpions showed that Bsaul1 contains all the residues which are highly conserved among long chain scorpion neurotoxins. Structural model of Bsaul1 was generated using Ts1 (a $\beta$-toxin that competes with the depressant insect toxins for binding to $Na^+$ channels) as template. According to the molecular model of Bsaul1, the folding of the polypeptide chain is being composed of an anti-parallel three-stranded $\beta$-sheet and a stretch of $\alpha$-helix, tightly bound by a set of four disulfide bridges. A striking similarity in the spatial arrangement of some critical residues was shown by superposition of the backbone conformation of Bsaul1 and Ts1.