• Title/Summary/Keyword: protein structures

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A Comparison of Three Dimensional Structures of Biosynthesized Preproinsulin and Insulin Using NMR

  • Oh, Mi-Na;Mok, K.-Hun;Lim, Yoong-Ho
    • Applied Biological Chemistry
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    • v.41 no.8
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    • pp.572-577
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    • 1998
  • The solution conformation of the human insulin precursor, preproinsulin, is described in terms of NMR spectral data. NMR experiments were performed on preproinsulin, whose structure was compared with the NMR structure of native human insulin. Despite the presence of the C-peptide and/or the signal peptide, secondary structure analyses indicate that the native structures of the A and B chains are well conserved even in preproinsulin. The observed relative robustness of the native structure in precursor forms permits further protein engineering experiments where the C-peptide or N-terminal signal sequence can be altered for the purpose of increasing expression or purification yields when producing recombinant human insulin.

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Synthesis and Characteristics of Porous Silica Ceramics with Organic Additives(I) (유기물 첨가에 따른 다공성 실리카 세라믹스의 제조 및 특성(I))

  • 신진용;이범재;노재성
    • Journal of the Korean Ceramic Society
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    • v.35 no.9
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    • pp.958-968
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    • 1998
  • Porous silica ceramics were prepared using DCCA(Drying Control Chemical Additives) Such as uncharged polymer(Polyethylene glycol) and protein (Lipase) under H2O/Low-grade TEOS=10 C2H5OH/Low-grade TEOS=1 HC1/Low=grade TEOS=0.01 After Plain which doesn't added DCCA and samples of 11 sorts which varied molecular weight of PEG(Mw=600, 1000, 2000) quantity of Lipase and concentration of wat-er were synthesized gellation time and thermal analysis were investigated. After heat-treated at 600, cry-stal structures analyses of SiO2 polymer and characteristics of pores were investigated. Gellation time was retarded about 2-6 times as compared with plain resulting in addition of DCCA and crystal structures ex-hibited amorphous state. Moreover as increase of water a short gellation time was obtained. The samples added PEG showed increase of specific surface areas up to 20-40% and had micropores while those of Lipase were decreased about 90% and showed broad pore size distribution.

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Analysis of Low Velocity Impact on Biomimetic Composites Mimicking Nacre (진주조개를 모방한 생체모방 복합재료의 저속충격 해석)

  • Jo, Seung-Un;Beom, Hyeon-Gyu
    • Composites Research
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    • v.23 no.4
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    • pp.1-6
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    • 2010
  • The dynamicresponse of biomimetic composites mimicking nacre under low velocity impact is investigated. The composites have hierarchical structures with a staggered pattern consisting of a protein and a mineral. To analyze the impact response of the composites, the finite element method is used. The effects of the hierarchical structures of the compositeson the dynamic response are examined. It is shown that the maximum stress, displacement and contact force in the composite subjected to low velocity impact decrease as the level of structural hierarchy increases.

Characterization of the $\alpha$-mannosidase Gene Family in Filamentous Fungi: N-glycan Remodelling for the Development of Eukaryotic Expression Systems

  • Eades, C.Joshua;Hintz, William E.
    • Biotechnology and Bioprocess Engineering:BBE
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    • v.5 no.4
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    • pp.227-233
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    • 2000
  • Although filamentous fungi are used extensively for protein expression, their use for the production of heterologous glycoproteins is constrained by the types of N-glycan structures produced by filamentous fungi as compared to those naturally found on the glycoproteins. Attempts are underway to engineer the N-glycan synthetic pathways in filamentous fungi in order to produce fungal expression strains which can produce heterologous glycoproteins carrying specific N-glycan structures. To fully realize this goal, a detailed understanding of the genetic components of this pathway in filamentous fungi is required. In this review, we discuss the characterization of the $\alpha$-mannosidase gene family in filamentous fungi and its implications for the elucidation of the N-glycan synthetic pathway.

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PreSMo Target-Binding Signatures in Intrinsically Disordered Proteins

  • Kim, Do-Hyoung;Han, Kyou-Hoon
    • Molecules and Cells
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    • v.41 no.10
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    • pp.889-899
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    • 2018
  • Intrinsically disordered proteins (IDPs) are highly unorthodox proteins that do not form three-dimensional structures under physiological conditions. The discovery of IDPs has destroyed the classical structure-function paradigm in protein science, 3-D structure = function, because IDPs even without well-folded 3-D structures are still capable of performing important biological functions and furthermore are associated with fatal diseases such as cancers, neurodegenerative diseases and viral pandemics. Pre-structured motifs (PreSMos) refer to transient local secondary structural elements present in the target-unbound state of IDPs. During the last two decades PreSMos have been steadily acknowledged as the critical determinants for target binding in dozens of IDPs. To date, the PreSMo concept provides the most convincing structural rationale explaining the IDP-target binding behavior at an atomic resolution. Here we present a brief developmental history of PreSMos and describe their common characteristics. We also provide a list of newly discovered PreSMos along with their functional relevance.

Crystal structure of mismatch repair protein MutS and its complex with a substrate DNA

  • Ban, Changill
    • Proceedings of the Korea Crystallographic Association Conference
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    • 2003.05a
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    • pp.16-16
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    • 2003
  • Mismatches in a DNA duplex are mainly due to DNA duplication errors that are generated by improper function of DNA polymerase. MutS, MutL and MutH are crucial proteins for the initiation of the methyl-directed mismatch repairing in bacteria. MutS has an ATPase activity md recognize the mismatched or unpaired bases on DNA. After binding to a mismatch, MutS recruits MutL to mediate the activation of MutH an endonuclease, which cleaves the 5' site of d(GATC) on the un-methylated strand. Both MutL and MutS also have essential roles in the subsequent removal and re-synthesis of the daughter strand. We have determined the crystal structures of either intact or active fragments of each of these proteins, both alone and complexed with ligands (DNA, ADP and ATP). The biochemical and mutagenesis studies based on the detailed 3-D structures led to new insights into the role of the ATPase activity of MutS in the mismatch recognition and directions for future investigation of mismatch repair.

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Analysis of the Structure-stability Relationship of Cold-adapted Lipase PsLip1 from Homology Modeling

  • Choo, Dong-Won
    • Genomics & Informatics
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    • v.9 no.2
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    • pp.79-84
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    • 2011
  • Two initial models of cold-adapted lipase PsLip1 have been constructed, based on homology with the bacterial lipases Chromobacterium viscosum (CvLip) and Pseudomonas cepacia (PcLip), whose X-ray structures have been solved and refined to high resolution. The mature polypeptide chains of these lipases have 84% similarity. The models of Mod1 and Mod2 have been compared with the tertiary structures of CvLip and PcLip, respectively, and analyzed in terms of stabilizing interactions. Several structural aspects that are believed to contribute to protein stability have been compared: the number of conserved salt bridges, aromatic interactions, hydrogen bonds, helix capping, and disulfide bridges. The 3-dimensional structural model of PsLip1 has been constructed in order to elucidate the structural reasons for the decreased thermostability of the enzyme in comparison with its mesophilic counterparts.

A Mini Review on Aβ Oligomers and its Pathogencity

  • Tuyet, Pham Thi Dieu
    • Journal of Integrative Natural Science
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    • v.7 no.2
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    • pp.79-86
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    • 2014
  • Amyloid oligomers are believed to play important causal roles in many types of amyloid-related degenerative diseases. Many different laboratories have reported amyloid oligomers that differ in size, morphology, toxicity, and method of preparation or purification, raising the question of the structural relationships among these oligomer preparations. The structural plasticity that has been reported to occur in amyloid formed from the same protein sequence indicates that it is quite possible that different oligomer preparations may represent distinct structural variants. In view of the difficulty in determining the precise structure of amyloids, conformation- and epitope-specific antibodies may provide a facile means of classifying amyloid oligomer structures. Conformation-dependent antibodies that recognize generic epitopes that are specifically associated with distinct aggregation states of many different amyloid-forming sequences indicate that there are at least two fundamentally distinct types of amyloid oligomers: fibrillar and prefibrillar oligomers. Classification of amyloid oligomers according to their underlying structures may be a more useful and rational approach than relying on differences in size and morphology.

Structure Prediction of Gasdermin a Receptor by Homology Modelling

  • Subathra Selvam
    • Journal of Integrative Natural Science
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    • v.16 no.3
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    • pp.97-102
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    • 2023
  • The gasdermins are a family of recently identified pore-forming effector proteins that cause membrane permeabilization and pyroptosis, a lytic pro-inflammatory type of cell death. A role in the regulation of cell proliferation and/or differentiation is suggested by the differentiation status-specific expression of gasdermin proteins in epithelial tissues. One of the GSDM protein is Gasdermin A (GSDMA), which decreased in stomach and esophageal cancers, suggesting a tumor suppressor role. GSDMA receptor antagonists have been researched as potential treatments for inflammatory diseases and baldness. GSDMA's significance in a wide range of disorders makes it an important therapeutic target. As a result, homology modelling of the GSDMA receptor was undertaken in the current study using the crystal structures of Mus musculus (GSDMA3), Human gasdermin D (GSDMD), and Murine gasdermin D (murine GSDMD). The best model was chosen based on the validation results after 20 models were developed utilising single template-based approaches. The generated structures can be used for further binding site and docking studies in the future.

Comparison of X-ray Crystallographic Structures and Docking Models of Dihydrofolate Reductase-Inhibitor Complexes (Dihydrofolate Reductase-저해제 복합체에 대한 X-선 결정체 구조와 docking model의 구조 비교)

  • 안미현;최인희;김춘미
    • YAKHAK HOEJI
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    • v.46 no.6
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    • pp.416-425
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    • 2002
  • A comparative study to validate the reliability of a fully automated docking program, FlexiDock, was carried out to predict the binding modes of DHFR-inhibitor complex. The inhibitors were extracted from the crystallographically determined DHFR-NADP$^{+}$(H)-inhibitor ternary complexes of human, Escherichia coli and Candida albicans and then docked back into the remaining DHFR-NADP$^{+}$(H) binary complexes using FlexiDock. The resulting conformations and orientations were compared to the original crystal complex structures for reproducibility. Then, folate, the substrate, and known inhibitors such as methotrexate, piritrexim and trimethoprim were docked into the wild-type human DHFR and their binding modes were compared with X-ray crystallographic or other modeling data. The root mean square deviations (RMSDs) for ligands ranged from 1.14 to 1.57$\AA$, and the protein backbone RMSDs from 0.94 to 1.26$\AA$. FlexiDock reproduced the orientations and binding modes of all seven ligands in good agreement with the crystal structures. It proved to be a reliable and efficient program in studying binding modes of DHFR-inhibitor complexes of different species, and the information obtained from this work may provide additional insight into the design of new agents with improved activity.ity.