• Title/Summary/Keyword: Molecular characterization

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Structural Design and Characterization of a Channel-forming Peptide

  • Krittanai, Chartchai;Panyim, Sakol
    • BMB Reports
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    • v.37 no.4
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    • pp.460-465
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    • 2004

  • A 16-residue polypeptide model with the sequence acetyl-YALSLAATLLKEAASL-OH was derived by rational de novo peptide design. The designed sequence consists of amino acid residues with high propensity to adopt an alpha helical conformation, and sequential order was arranged to produce an amphipathic surface. The designed sequence was chemically synthesized using a solid-phase method and the polypeptide was purified by reverse-phase liquid chromatography. Molecular mass analysis by electro-spray ionization mass spectroscopy confirmed the correct designed sequence. Structural characterization by circular dichroism spectroscopy demonstrated that the peptide adopts the expected alpha helical conformation in 50% acetonitrile solution. Liposome binding assay using Small Unilamellar Vesicle (SUV) showed a marked release of entrapped glucose by interaction between the lipid membrane and the tested peptide. The channel-forming activity of the peptide was revealed by a planar lipid bilayer experiment. An analysis of the conducting current at various applied potentials suggested that the peptide forms a cationic ion channel with an intrinsic conductance of 188 pS. These results demonstrate that a simple rational de novo design can be successfully employed to create short peptides with desired structures and functions.

  • https://doi.org/10.5483/BMBRep.2004.37.4.460 인용 PDF

Synthesis of Hβ (core)/SAPO-11 (shell) Composite Molecular Sieve and its Catalytic Performances in the Methylation of Naphthalene with Methanol

  • Wang, Xiaoxiao;Guo, Shaoqing;Zhao, Liangfu
    • Bulletin of the Korean Chemical Society
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    • v.34 no.12
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    • pp.3829-3834
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    • 2013

  • $H{\beta}$ (core)/SAPO-11 (shell) composite molecular sieve was synthesized by the hydrothermal method in order to combine the advantages of $H{\beta}$ and SAPO-11 for the methylation of naphthalene with methanol. For comparison, the mechanical mixture was prepared through the blending of $H{\beta}$ and SAPO-11. The physicochemical properties of $H{\beta}$, SAPO-11, the composite and the mechanical mixture were characterized by various characterization methods. The characterization results indicated that $H{\beta}$/SAPO-11 composite molecular sieve exhibited a core-shell structure, with the $H{\beta}$ phase as the core and the SAPO-11 phase as the shell. The pore diameter of the composite was between that of $H{\beta}$ and SAPO-11. The composite had fewer acid sites than $H{\beta}$ and mechanical mixture while more acid sites than SAPO-11. The experimental results indicated that the composite exhibited high catalytic performances for the methylation of naphthalene with methanol.

  • https://doi.org/10.5012/bkcs.2013.34.12.3829 인용 PDF KSCI KPUBS HTML

Molecular Cloning and Characterization of Chymotrypsin Inhibitor and Chitin-Binding Protein Homologs from the Bumblebee Bombus terrestris

  • Qiu, Yuling;Yoon, Hyung-Joo;Jin, Byung-Rae
    • International Journal of Industrial Entomology and Biomaterials
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    • v.25 no.1
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    • pp.115-121
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    • 2012

  • The bumblebee Bombus terrestris is widely used in greenhouses to pollinate crops. Here, we report the molecular cloning and characterization of chymotrypsin inhibitor and chitin-binding protein homologs from B. terrestris. Two cDNAs encoding chymotrypsin inhibitor (Bt-CI) and chitin-binding protein (Bt-CBP) homologs were cloned from B. terrestris. Gene sequence analysis showed that Bt-CI gene consists of three exons encoding 75 amino acids, including a predicted 20-amino acid signal peptide, while Bt-CBP consists of two exons encoding 78 amino acids, including a predicted 26-amino acid signal peptide. The mature Bt-CI and Bt-CBP peptides contain ten and six conserved cysteine residues, respectively. Database searches using the deduced sequences of Bt-CI and Bt-CBP showed similarity to those from B. impatiens (96% peptide sequence identities). Bt-CI and Bt-CBP were expressed in both the venom gland and fat body of B. terrestris worker bees. The recombinant Bt-CI and Bt-CBP peptides were expressed in baculovirus-infected insect cells. Taken together, our findings describe the molecular characterization of Bt-CI and Bt-CBP from B. terrestris.

  • https://doi.org/10.7852/ijie.2012.25.1.115 인용 PDF KSCI