• Title/Summary/Keyword: Secondary resonance

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NMR study on secondary metabolites isolated from an identified tunicate

  • Rho, Jung-Rae
    • Journal of the Korean Magnetic Resonance Society
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    • v.8 no.2
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    • pp.115-126
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    • 2004
  • Four secondary metabolites from an unidentified tunicate were isolated by treatment with trichloroethyl chloroformate(TECF) or acetic anhydride in pyridine. Their structures were determined by an extensive NMR analysis and the configuration of diacetyl derivatives(3a, 4a) was assigned by comparing with NMR data of a similar compound. Three new naturally occurring compounds (1, 3, 4) showed potent brine shrimp lethality and antifungal effect against Candia albicans.

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$^{11}B$ Quadrupole Interaction Studies of Boron-doped Graphite Electrode for Lithium Secondary Battery

  • Lee, Youngil;Han, Duk-Young;Lee, Donghoon;Woo, Ae-Ja;Lee, Sam-Hyeon;Kim, Kyung-Han;Lee, Man-Ho
    • Journal of the Korean Magnetic Resonance Society
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    • v.3 no.2
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    • pp.90-99
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    • 1999
  • Doping of boron atoms in graphite has been well known method to increase the discharge capacity as the negative electrode material for lithium secondary battery. Herein, the boron-doped graphites are prepared by mixing 1, 2.5, 5, and 7 wt. % of boron carbide in carbon during the graphitizing process. The structural states of boron in boron-doped graphites are investigated by solid-state 11B NMR spectroscopy. The resonance lines for substitutional boron atoms are identified as the second order quadrupolar powder pattern with the quardrupole coupling constant, QCC = 3.36(2) MHz. The quantitative analysis of 11B NMR spectra with boron-doped graphite has also been performed via simulation.

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Backbone assignment of the anticodon binding domain of human Glycyl-tRNA synthetase

  • Mushtaq, Ameeq Ul;Cho, Hye Young;Byun, Youngjoo;Jeon, Young Ho
    • Journal of the Korean Magnetic Resonance Society
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    • v.20 no.2
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    • pp.50-55
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    • 2016
  • Backbone $^1H$, $^{13}C$ and $^{15}N$ resonance assignments are presented for the anticodon binding domain (residues 557-674) of human glycyl-tRNA synthetase (GRS). Role of the anticodon binding domain (ABD) of GRS as an anticancer ligand has recently been reported and its role in other diseases like Charcot-Marie-Tooth (CMT) and polymyositis have increased its interest. NMR assignments were completed using the isotope [$^{13}C/^{15}N$]-enriched protein and chemical shifts based secondary structure analysis with TALOS+ demonstrate similar secondary structure as reported in X-ray structure PDB 2ZT8, except some C-terminal residues. NMR signals from the N-terminal residues 557 to 571 and 590 to 614 showed very weak or no signals exhibiting dynamics or conformational exchange in NMR timescale.

1H, 15N, and 13C backbone assignments and secondary structure of the cytoplasmic domain A of mannitol trasporter IIMannitol from Thermoanaerobacter Tencongensis phosphotransferase system

  • Lee, Ko-On;Suh, Jeong-Yong
    • Journal of the Korean Magnetic Resonance Society
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    • v.19 no.1
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    • pp.42-48
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    • 2015
  • The mannitol transporter Enzyme $II^{Mtl}$ of the bacterial phosphotransferase system has two cytoplasmic phosphoryl transfer domains $IIA^{Mtl}$ and $IIB^{Mtl}$. The two domains are linked by a flexible peptide linker in mesophilic bacterial strains, whereas they are expressed as separated domains in thermophilic strains. Here, we carried out backbone assignment of $IIA^{Mtl}$ from thermophilic Thermoanaerobacter Tencongensis using a suite of heteronuclear triple resonance NMR spectroscopy. We have completed 94% of the backbone assignment, and obtained secondary structural information based on torsion angles derived from the chemical shifts. $IIA^{Mtl}$ of Thermoanaerobacter Tencongensis is predicted to have six ${\beta}$ strands and six ${\alpha}$ helices, which is analogous to $IIA^{Mtl}$ of Escherichia coli.

Auto-parametric resonance of framed structures under periodic excitations

  • Li, Yuchun;Gou, Hongliang;Zhang, Long;Chang, Chenyu
    • Structural Engineering and Mechanics
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    • v.61 no.4
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    • pp.497-510
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    • 2017
  • A framed structure may be composed of two sub-structures, which are linked by a hinged joint. One sub-structure is the primary system and the other is the secondary system. The primary system, which is subjected to the periodic external load, can give rise to an auto-parametric resonance of the second system. Considering the geometric-stiffness effect produced by the axially internal force, the element equation of motion is derived by the extended Hamilton's principle. The element equations are then assembled into the global non-homogeneous Mathieu-Hill equations. The Newmark's method is introduced to solve the time-history responses of the non-homogeneous Mathieu-Hill equations. The energy-growth exponent/coefficient (EGE/EGC) and a finite-time Lyapunov exponent (FLE) are proposed for determining the auto-parametric instability boundaries of the structural system. The auto-parametric instabilities are numerically analyzed for the two frames. The influence of relative stiffness between the primary and secondary systems on the auto-parametric instability boundaries is investigated. A phenomenon of the "auto-parametric internal resonance" (the auto-parametric resonance of the second system induced by a normal resonance of the primary system) is predicted through the two numerical examples. The risk of auto-parametric internal resonance is emphasized. An auto-parametric resonance experiment of a ${\Gamma}$-shaped frame is conducted for verifying the theoretical predictions and present calculation method.

1H, 15N and 13C resonance assignment and secondary structure prediction of ss-DNA binding protein 12RNP2 precursor, HP0827 from Helicobacter pylori

  • Jang, Sun-Bok;Ma, Chao;Chandan, Pathak Chinar;Kim, Do-Hee;Lee, Bong-Jin
    • Journal of the Korean Magnetic Resonance Society
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    • v.15 no.1
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    • pp.69-79
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    • 2011
  • HP0827 has two RNP motif which is a very common protein domain involved in recognition of a wide range of ssRNA/DNA.We acquired 3D NMR spectra of HP0827 which shows well dispersed and homogeneous signals which allows us to assign 98% of all $^1H_N$, $^{15}N$, $^{13}C_{\alpha}$, $^{13}C_{\beta}$ and $^{13}C$=O resonances and 90% of all sidechain resonances. The sequence-specific backbone resonance assignment of HP0827 can be used to gain deeper insights into the nucleic acids binding specificity of HP0827 in the future study. Here, we report secondary structure prediction of HP0827 derived from NMR data. Additionally, ssRNA/DNA binding assay studies was also conducted. This study might provide a clue for exact function of HP0827 based on structure and sequence.

Structural Characterization of the J-domain of Tid1, a Mitochondrial Hsp40/DnaJ Protein

  • Sim, Dae-Won;Jo, Ku-Sung;Ryu, Kyoung-Seok;Kim, Eun-Hee;Won, Hyung-Sik
    • Journal of the Korean Magnetic Resonance Society
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    • v.16 no.1
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    • pp.22-33
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    • 2012
  • Tid1, belonging to the Hsp40/DnaJ family of proteins, functions as a cochaperone of cytosolic and mitochondrial Hsp70 proteins. In particular, the N-terminal J-domain of Tid1 (Tid1-JD) constitutes the major binding sites for proteinprotein interactions with client proteins, including p53, as well as its partner chaperone, Hsp70. In the present study, soluble, recombinant protein of Tid1-JD could be obtained by using the pCold vector system, and backbone NMR assignments were completed using the isotope $[^{13}C/^{15}N]$-enriched protein. Far-UV CD result implied that Tid1-JD is an ${\alpha}$-helical protein and the secondary structure determined using chemical shift data sets indentified four ${\alpha}$-helices with a loop region containing the HPD (conserved tripeptide of His, Pro and Asp) motif. Additionally, NMR spectra under different conditions implied that the HPD motif, which is a critical region for protein-protein interactions of Tid1-JD, would possess dynamic properties.

Secondary resonances of a microresonator under AC-DC electrostatic and DC piezoelectric actuations

  • Zamanian, M.;Hosseini, S.A.A.
    • Structural Engineering and Mechanics
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    • v.42 no.5
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    • pp.677-699
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    • 2012
  • This article studies the secondary resonances of a clamped-clamped microresonator under combined electrostatic and piezoelectric actuations. The electrostatic actuation is induced by applying the AC-DC voltage between the microbeam and the electrode plate that lies at the opposite side of the microbeam. The piezoelectric actuation is induced by applying the DC voltage between upper and lower sides of piezoelectric layer. It is assumed that the neutral axis of bending is stretched when the microbeam is deflected. The drift effect of piezoelectric layer (the phenomenon where there is a slow increase of the free strain after the application of a DC field) is neglected. The equations of motion are solved by using the multiple scale perturbation method. The system possesses a subharmonic resonance of order one-half and a superharmonic resonance of order two. It is shown that using the DC piezoelectric actuation, the sensitivity of AC-DC electrostatically actuated microresonator under subharmonic and superharmonic resonances may be tuned. In addition, it is shown that the tuning domain of the microbeam under combined electrostatic and piezoelectric actuations at subharmonic and superharmonic conditions is larger than the tuning domain of microbeam under only the electrostatic actuation.