• Title/Summary/Keyword: In-folding Structure

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A Research of Chima in the Chosun Dynasty (조선조 치마 재고)

  • 박성실
    • Journal of the Korean Society of Costume
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    • v.30
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    • pp.295-306
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    • 1996
  • A large quantity of exhumed clothing found for recent 20 years has becom-e the material for making a concrete clarification of the structure of clothing in the Chosun dynasty. Exhumed clothing means the clothing found in the coffin when the grave of the ancestor buried several hundred several hundred years ago is removed to another pla-ce and it is almost comprised of ordinary clothes of the grave-owner not mourning clothes as well as clothing and ornaments in the period between the 15th cen-tury and th 19th century. This research is intended to inquire into the kind of chimas in the 16th century before the Imjin Japancese Invasion of Korea during 1592-1598. The after effect of the Imjin Japanese In-vasion was generally reflected in clothing them and the structure of clothing in the Chosun dynasty began to overshadew its di-chotomy with the Imjin Japanese I vasion of Korea as the point. Accordingly this research is concerned with the study of the chima system of the early Chosun dynasty which shows that there is a common point of the identical form though clothing was exhumed in different graves. Therefore it was possible to grasp women's clothing that was fashionable at that time The object for research is the women in the upper class of the 16th century whose representative characteristics are depicted as follows: 1. Women in the upper class wore the splendid clothing similar to the ordinary clothing of court ladies. 2. The division of ordinary chima and ceremonial chima appeared in the concrete. 3. Ceremonial chima had its extra width and length and exhibited its exaggerated silhouette. in particular it had a various forms of over-pleats made at its center front which play a role in supplementing discomfort in walking. This associate bustle and crinolin styles through which the modern design of clothing can be glimpsed. 4. The opposite phenomenon was shown that has been perceived up to now such as folding at the right plain seam the treatment of the edge-and the like. 5. The elaboration of manual needlework shows the culmination of women's workmanship.

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Thermal Stability of Phaseolus vulgaris Leucoagglutinin: a Differential Scanning Calorimetry Study

  • Biswas, Shyamasri;Kayastha, Arvind M.
    • BMB Reports
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    • v.35 no.5
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    • pp.472-475
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    • 2002
  • Phaseolus vulgaris phytohemagglutinin L is a homotetrameric-leucoagglutinating seed lectin. Its three-dimensional structure shows similarity with other members of the legume lectin family. The tetrameric form of this lectin is pH dependent. Gel filtration results showed that the protein exists in its dimeric state at pH 2.5 and as a tetramer at pH 7.2. Contrary to earlier reports on legume lectins that possess canonical dimers, thermal denaturation studies show that the refolding of phytohemagglutinin L at neutral pH is irreversible. Differential scanning calorimetry (DSC) was used to study the denaturation of this lectin as a function of pH that ranged from 2.0 to 3.0. The lectin was found to be extremely thermostable with a transition temperature around $82^{\circ}C$ and above $100^{\circ}C$ at pH 2.5 and 7.2, respectively. The ratio of calorimetric to vant Hoff enthalpy could not be calculated because of its irreversible-folding behavior. However, from the DSC data, it was discovered that the protein remains in its compact-folded state, even at pH 2.3, with the onset of denaturation occurring at $60^{\circ}C$.

Engineering Hybrid Proteins by Modular Recombination and Evolutionary Optimization (모듈성 단백질의 재설계 및 개량)

  • Lee, Seung-Goo;Rha, Eu-Gene;Ha, Jae-Seok;Lee, Jeong-Min;Kim, Sun-Hwa
    • Microbiology and Biotechnology Letters
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    • v.36 no.2
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    • pp.149-157
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    • 2008
  • Many proteins consist of distinctive domains that can act independently or cooperatively to achieve a unique function. As these domains evolve from a naturally existing repertoire of functional domains, this implies that domain organization is an intrinsic element involved in building the complex structure and function of proteins. Thus, identifying functional domains would appear to be critical to the elucidation of questions related to protein evolution, folding, and the engineering of hybrid proteins for tai- lored applications. However, the simple application of "Lego-like assembly" to the engineering of hybrid proteins is an oversimplification, as many hybrid constructs lack structural stability, usually due to unfavorable domain contacts. Thus, directed evolution, along with computational studies, may help to engineer hybrid proteins with improved physico-chemical properties. Accordingly, this paper introduces several approaches to functional hybrid protein engineering that potentially can be used to create modulators of gene transcription and cell signaling, and novel biosensors to analyze biological functions in vivo.

Fabrication of Folded Monopole Antenna for Quintuple Band Mobile Phone Handset (5밴드 휴대폰용 폴디드 모노폴 안테나 제작)

  • Jang In-Seok;Son Tae-Ho;Lee Jae-Ho
    • The Journal of Korean Institute of Electromagnetic Engineering and Science
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    • v.17 no.8 s.111
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    • pp.713-718
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    • 2006
  • We designed and fabricated, in this paper, a quintuple band folded monopole antenna for the mobile phone handset that can be provided multiple mobile services. Antenna design was based on the compensation of series antenna capacitance with the expansion of physical antenna length by the proper folding structure. It's shown that this antenna satisfies quintuple service band as CDMA/GSM/DCS/USPCS/WCDMA, and is more cost competitive than conventional metal plate pressing method by applying on flexible PCB technology. Measured maximum gain on quintuple band were $-2.51{\sim}+1.82 dBi$, and radiation patterns were also shown nearly omnidirectional on all bands.

Leaf-specific pathogenesis-related 10 homolog, PgPR-10.3, shows in silico binding affinity with several biologically important molecules

  • Han, Jin Haeng;Lee, Jin Hee;Lee, Ok Ran
    • Journal of Ginseng Research
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    • v.39 no.4
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    • pp.406-413
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    • 2015
  • Background: Pathogenesis-related 10 (PR-10) proteins are small, cytosolic proteins with a similar three-dimensional structure. Crystal structures for several PR-10 homologs have similar overall folding patterns, with an unusually large internal cavity that is a binding site for biologically important molecules. Although structural information on PR-10 proteins is substantial, understanding of their biological function remains limited. Here, we showed that one of the PgPR-10 homologs, PgPR-10.3, shares binding properties with flavonoids, kinetin, emodin, deoxycholic acid, and ginsenoside Re (1 of the steroid glycosides). Methods: Gene expression patterns of PgPR-10.3 were analyzed by quantitative real-time PCR. The three-dimensional structure of PgPR-10 proteins was visualized by homology modeling, and docking to retrieve biologically active molecules was performed using AutoDock4 program. Results: Transcript levels of PgPR-10.3 expressed in leaves, stems, and roots of 3-wk-old ginseng plantlets were on average 86-fold lower than those of PgPR-10.2. In mature 2-yr-old ginseng plants, the mRNA of PgPR-10.3 is restricted to leaves. Ginsenoside Re production is especially prominent in leaves of Panax ginseng Meyer, and the binding property of PgPR-10.3 with ginsenoside Re suggests that this protein has an important role in the control of secondary metabolism. Conclusion: Although ginseng PR-10.3 gene is expressed in all organs of 3-wk-old plantlets, its expression is restricted to leaves in mature 2-yr-old ginseng plants. The putative binding property of PgPR-10.3 with Re is intriguing. Further verification of binding affinity with other biologically important molecules in the large hydrophobic cavity of PgPR-10.3 may provide an insight into the biological features of PR-10 proteins.

Identification of Alkylation-Sensitive Target Chaperone Proteins and Their Reactivity with Natural Products Containing Michael Acceptor

  • Liu, Xi-Wen;Sok, Dai-Eun
    • Archives of Pharmacal Research
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    • v.26 no.12
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    • pp.1047-1054
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    • 2003
  • Molecular chaperones have a crucial role in the folding of nascent polypeptides in endoplasmic reticulum. Some of them are known to be sensitive to the modification by electrophilic metabolites of organic pro-toxicants. In order to identify chaperone proteins sensitive to alkyators, ER extract was subjected to alkylation by 4-acetamido-4 -maleimidyl-stilbene-2,2 -disulfonate (AMS), and subsequent SDS-PAGE analyses. Protein spots, with molecular mass of 160, 100, 57 and 36 kDa, were found to be sensitive to AMS alkylation, and one abundant chaperon protein was identified to be protein disulfide isomerase (PDI) in comparison with the purified PDI. To see the reactivity of PDI with cysteine alkylators, the reduced form ($PDI_{red}$) of PDI was incubated with various alkylators containing Michael acceptor structure for 30 min at $38^{\circ}C$ at pH 6.3, and the remaining activity was determined by the insulin reduction assay. Iodoacetamide or N-ethylmaleimide at 0.1 mM remarkably inactivated $PDI_{red}$ with N-ethylmaleimide being more potent than iodoacetamide. A partial inactivation of $PDI_{oxid}$ was expressed by iodoacetamide, but not N-ethylmaleimide (NEM) at pH 6.3. Of Michael acceptor compounds tested, 1,4-benzoquinone ($IC_{50}, 15 \mu$ M) was the most potent, followed by 4-hydroxy-2-nonenal and 1,4-naphthoquinone. In contrast, 1,2-naphthoquinone, devoid of a remarkable inactivation action, was effective to cause the oxidative conversion of $PDI_{red}$ to $PDI_{oxid}$. Thus, the action of Michael acceptor compounds differed greatly depending on their structure. Based on these, it is proposed that POI, one of chaperone proteins in ER, could be susceptible to endogenous or xenobiotic Michael acceptor compounds in vivo system.

Higher Order Structure of 5S rRNA from Xanthomonas palargonii (Xanthomonas palargonii 5S rRNA의 고차원 구조)

  • Cho, Bongrae;Kim, Sang Bumn;Lee, Younghoon;Park, Inwon
    • Journal of the Korean Chemical Society
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    • v.39 no.9
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    • pp.734-740
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    • 1995
  • The primary and secondary structures of Xanthomonas palargonii 5S rRNA were determined. The higher order structure of the 5S rRNA was also analysed using several ribonucleases and chemical probes, such as ethylnitrourea, Pb2+, dimethylsulfate and diethyl pyrocarbonate. Ethylnitrourea was used for probing the phosphate groups involved in the tertiary interactions in the 5S rRNA. Nucleotides G72, A73, G75, A78, G98, G100 and A101 in unstable helical region d, nucleotides C36, C37, A39, and C41 in loop c, nucleotides A29 and G33 in stem C became resistant to ethylnitrourea modification in the presence of Mg2+. On the basis of findings from chemical and enzymatic studies, and also Pb2+-induced cleavages, it was concluded that region b-C and unstable helical region d may act as hinges in the folding of 5S rRNA.

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Virtual Screening and Testing of GSK-3 Inhibitors Using Human SH-SY5Y Cells Expressing Tau Folding Reporter and Mouse Hippocampal Primary Culture under Tau Cytotoxicity

  • Chih-Hsin Lin;Yu-Shao Hsieh;Ying-Chieh Sun;Wun-Han Huang;Shu-Ling Chen;Zheng-Kui Weng;Te-Hsien Lin;Yih-Ru Wu;Kuo-Hsuan Chang;Hei-Jen Huang;Guan-Chiun Lee;Hsiu Mei Hsieh-Li;Guey-Jen Lee-Chen
    • Biomolecules & Therapeutics
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    • v.31 no.1
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    • pp.127-138
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    • 2023
  • Glycogen synthase kinase-3β (GSK-3β) is an important serine/threonine kinase that implicates in multiple cellular processes and links with the neurodegenerative diseases including Alzheimer's disease (AD). In this study, structure-based virtual screening was performed to search database for compounds targeting GSK-3β from Enamine's screening collection. Of the top-ranked compounds, 7 primary hits underwent a luminescent kinase assay and a cell assay using human neuroblastoma SH-SY5Y cells expressing Tau repeat domain (TauRD) with pro-aggregant mutation ΔK280. In the kinase assay for these 7 compounds, residual GSK-3β activities ranged from 36.1% to 90.0% were detected at the IC50 of SB-216763. In the cell assay, only compounds VB-030 and VB-037 reduced Tau aggregation in SH-SY5Y cells expressing ΔK280 TauRD-DsRed folding reporter. In SH-SY5Y cells expressing ΔK280 TauRD, neither VB-030 nor VB-037 increased expression of GSK-3α Ser21 or GSK-3β Ser9. Among extracellular signal-regulated kinase (ERK), AKT serine/threonine kinase 1 (AKT), mitogen-activated protein kinase 14 (P38) and mitogenactivated protein kinase 8 (JNK) which modulate Tau phosphorylation, VB-037 attenuated active phosphorylation of P38 Thr180/ Tyr182, whereas VB-030 had no effect on the phosphorylation status of ERK, AKT, P38 or JNK. However, both VB-030 and VB-037 reduced endogenous Tau phosphorylation at Ser202, Thr231, Ser396 and Ser404 in neuronally differentiated SH-SY5Y expressing ΔK280 TauRD. In addition, VB-030 and VB-037 further improved neuronal survival and/or neurite length and branch in mouse hippocampal primary culture under Tau cytotoxicity. Overall, through inhibiting GSK-3β kinase activity and/or p-P38 (Thr180/Tyr182), both compounds may serve as promising candidates to reduce Tau aggregation/cytotoxicity for AD treatment.

A Novel Strategy for Thermostability Improvement of Trypsin Based on N-Glycosylation within the Ω-Loop Region

  • Guo, Chao;Liu, Ye;Yu, Haoran;Du, Kun;Gan, Yiru;Huang, He
    • Journal of Microbiology and Biotechnology
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    • v.26 no.7
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    • pp.1163-1172
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    • 2016
  • The Ω-loop is a nonregular and flexible structure that plays an important role in molecular recognition, protein folding, and thermostability. In the present study, molecular dynamics simulation was carried out to assess the molecular stability and flexibility profile of the porcine trypsin structures. Two Ω-Loops (fragment 57-67 and fragment 78-91) were confirmed to represent the flexible region. Subsequently, glycosylation site-directed mutations (A73S, N84S, and R104S) were introduced within the Ω-loop region and its wing chain based on its potential N-glycosylation sites (Asn-Xaa-Ser/Thr consensus sequences) and structure information to improve the thermostability of trypsin. The result demonstrated that the half-life of the N84S mutant at 50℃ increased by 177.89 min when compared with that of the wild-type enzyme. Furthermore, the significant increase in the thermal stability of the N84S mutant has also been proven by an increase in the Tm values determined by circular dichroism. Additionally, the optimum temperatures of the wild-type enzyme and the N84S mutant were 75℃ and 80℃, respectively. In conclusion, we obtained the thermostability-improved enzyme N84S mutant, and the strategy used to design this mutant based on its structural information and N-linked glycosylation modification could be applied to engineer other enzymes to meet the needs of the biotechnological industry.

Solution structure and functional analysis of HelaTx1: the first toxin member of the κ-KTx5 subfamily

  • Park, Bong Gyu;Peigneur, Steve;Esaki, Nao;Yamaguchi, Yoko;Ryu, Jae Ha;Tytgat, Jan;Kim, Jae Il;Sato, Kazuki
    • BMB Reports
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    • v.53 no.5
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    • pp.260-265
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    • 2020
  • Scorpion venom comprises a cocktail of toxins that have proven to be useful molecular tools for studying the pharmacological properties of membrane ion channels. HelaTx1, a short peptide neurotoxin isolated recently from the venom of the scorpion Heterometrus laoticus, is a 25 amino acid peptide with two disulfide bonds that shares low sequence homology with other scorpion toxins. HelaTx1 effectively decreases the amplitude of the K+ currents of voltage-gated Kv1.1 and Kv1.6 channels expressed in Xenopus oocytes, and was identified as the first toxin member of the κ-KTx5 subfamily, based on a sequence comparison and phylogenetic analysis. In the present study, we report the NMR solution structure of HelaTx1, and the major interaction points for its binding to voltage-gated Kv1.1 channels. The NMR results indicate that HelaTx1 adopts a helix-loop-helix fold linked by two disulfide bonds without any β-sheets, resembling the molecular folding of other cysteine-stabilized helix-loop-helix (Cs α/α) scorpion toxins such as κ-hefutoxin, HeTx, and OmTx, as well as conotoxin pl14a. A series of alanine-scanning analogs revealed a broad surface on the toxin molecule largely comprising positively-charged residues that is crucial for interaction with voltage-gated Kv1.1 channels. Interestingly, the functional dyad, a key molecular determinant for activity against voltage-gated potassium channels in other toxins, is not present in HelaTx1.