• Title/Summary/Keyword: Magnetic Domains

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Mainchain NMR Assignments and secondary structure prediction of the C-terminal domain of BldD, a developmental transcriptional regulator from Streptomyces coelicolor A3(2)

  • Kim, Jeong-Mok;Won, Hyung-Sik;Kang, Sa-Ouk
    • Journal of the Korean Magnetic Resonance Society
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    • v.17 no.1
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    • pp.59-66
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    • 2013
  • BldD, a developmental transcription factor from Streptomyces coelicolor, is a homodimeric, DNA-binding protein with 167 amino acids in each subunit. Each monomer consists of two structurally distinct domains, the N-terminal domain (BldD-NTD) responsible for DNA-binding and dimerization and the C-terminal domain (BldD-CTD). In contrast to the BldD-NTD, of which crystal structure has been solved, the BldD-CTD has been characterized neither in structure nor in function. Thus, in terms of structural genomics, structural study of the BldD-CTD has been conducted in solution, and in the present work, mainchain NMR assignments of the recombinant BldD-CTD (residues 80-167 of BldD) could be achieved by a series of heteronuclear multidimensional NMR experiments on a [$^{13}C/^{15}N$]-enriched protein sample. Finally, the secondary structure prediction by CSI and TALOS+ analysis using the assigned chemical shifts data identified a ${\beta}-{\alpha}-{\alpha}-{\beta}-{\alpha}-{\alpha}-{\alpha}$ topology of the domain. The results will provide the most fundamental data for more detailed approach to the atomic structure of the BldD-CTD, which would be essential for entire understanding of the molecular function of BldD.

Expression, Purification and NMR studies of SH3YL1 SH3 domain

  • Shrestha, Pravesh;Yun, Ji-Hye;Lee, Weon-Tae
    • Journal of the Korean Magnetic Resonance Society
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    • v.14 no.2
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    • pp.105-116
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    • 2010
  • SH3YL1, a novel protein containing one Src homology 3 domain at the carboxyl terminus was first detected in mouse anagen skin cDNA. This protein had a significant homology with YHRO 16c/Ysc 84, the yeast Src homology 3 domain-containing protein. The sequence identity was remarkable at the carboxyl and amino-terminal Src homology 3 domain, suggesting that the novel protein is a mouse homolog of the yeast protein and thus was termed as SH3YL1. SH3YL1 is composed of two domains, a DUF500 at N-termini and a SH3 domain at C-termini. In our study we cloned the SH3 domain in bacterial expression system in Escherichia coli using pET32a vector with TEV protease cleavage site and purified as a monomer using affinity chromatography. The N-terminal poly-Histidine tag was cleaved with TEV protease and target protein was used for backbone studies. Our study showed that SH3 domain primarily consists of $\beta$-sheet which is in consistence with previous result performed on the truncated SH3 domain of SH3YL1.

Temperature Dependence of The Magnetoimpedence Effect in Nanocrystalline $Fe_{84}Zr_7B_6Cu_1Al_2$ Alloy

  • Kwon, Hye-Suk;Lee, Heebok;Kim, Yong-Kook;Yoon, Sung-Ho;Kim, Taik-Kee;Yu, Seong-Cho
    • Proceedings of the Korean Magnestics Society Conference
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    • 2000.09a
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    • pp.473-479
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    • 2000
  • The nanocrystalline Fe$_{84}$Zr$_{7}$B$_{6}$Cu$_{1}$ $Al_{2}$ alloy was annealed at 450 $^{\circ}C$ and 550 $^{\circ}C$ for l hour to achieve the ultra-soft magnetic properties such as large magnetoimpedence ratio(MIR), the incremental permeability ratio(PR), nearly zero coercivity, zero magnetostriction, etc. The PR and MIR of the sample were measured from 100 kHz to 10 MHz at a cryogenic chamber where the temperature can be varie from 10 K to 300 K. The increment of MIR value is proportional to increasing temperature. The maximum PR values measured at high frequency above 1 MHz remain almost same despite of the temperature variation from 10 K to 300 K except the sharpness in PR curves. However, the maximum PR values measured below 1 MHz show drastic increment at above 150K due to thermal activation of magnetic domains.s.s.

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THE EFFECTS OF ANNEALING ON THE DC MAGNETIC PROPERTIES OF AN IRON-BASED AMORPHOUS ALLOY

  • Choi, Y.S.;Kim, D.H.;Lim, S.H.;Noh, T.H.;Kang, I.K.
    • Journal of the Korean Magnetics Society
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    • v.5 no.5
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    • pp.478-482
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    • 1995
  • The iron-based Metglas 2605S3A amorphous alloy ribbons are annealed at $435^{\circ}C$ for various periods from 5 to 210 min, and the effect of annealing is investigated on the dc magnetic properties of the ribbon. Typical square-type hysteresis loops are observed for the ribbons annealed fo 5 min, indicative of the nearly complete removal of residual stresses which are produced during melt-quenching. As the annealing time increases, the coercivity increases and the shape of hysteresis loops transforms to round type and finally to sheared one at the longest annealing time of 210 min. These results may be explained by the formation of clusters with chemical shortorder and very fine crystallites (at the annealing time of 210 min), and the diffusion-induced stresses during the formation of the clusters. For the samples annealed for 5 min, very good dc properties of the squareness ratio, coercivity and maximum permeability are observed, but, rather unexpectedly, the initial permeability is found to be very low. These results are considered to be due to a simple domain structure consisting of very small number of $^{\circ}$ domains.

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Hyperpolarized Carbon-13 Magnetic Resonance Imaging: Technical Considerations and Clinical Applications

  • Ying-Chieh Lai;Ching-Yi Hsieh;Yu-Hsiang Juan;Kuan-Ying Lu;Hsien-Ju Lee;Shu-Hang Ng;Yung-Liang Wan;Gigin Lin
    • Korean Journal of Radiology
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    • v.25 no.5
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    • pp.459-472
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    • 2024
  • Hyperpolarized (HP) carbon-13 (13C) MRI represents an innovative approach for noninvasive, real-time assessment of dynamic metabolic flux, with potential integration into routine clinical MRI. The use of [1-13C]pyruvate as a probe and its conversion to [1-13C]lactate constitute an extensively explored metabolic pathway. This review comprehensively outlines the establishment of HP 13C-MRI, covering multidisciplinary team collaboration, hardware prerequisites, probe preparation, hyperpolarization techniques, imaging acquisition, and data analysis. This article discusses the clinical applications of HP 13C-MRI across various anatomical domains, including the brain, heart, skeletal muscle, breast, liver, kidney, pancreas, and prostate. Each section highlights the specific applications and findings pertinent to these regions, emphasizing the potential versatility of HP 13C-MRI in diverse clinical contexts. This review serves as a comprehensive update, bridging technical aspects with clinical applications and offering insights into the ongoing advancements in HP 13C-MRI.

Biotinoyl Domain of Human Acetyl-CoA Carboxylase;Structural Insights into the Carboxyl Transfer Mechanism

  • Lee, Chung-Kyung;Cheong, Hae-Kap;Ryu, Kyoung-Seok;Lee, Jae-Il;Jeon, Young-Ho;Cheong, Chae-Joon
    • Journal of the Korean Magnetic Resonance Society
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    • v.12 no.1
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    • pp.1-13
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    • 2008
  • Acetyl-CoA carboxylase (ACC) catalyzes the first step in fatty acid biosynthesis: the synthesis of malonyl-CoA from acetyl-CoA. As essential regulators of fatty acid biosynthesis and metabolism, ACCs are regarded as therapeutic targets for the treatment of metabolic diseases such as obesity, In ACC, the biotinoyl domain performs a critical function by transferring an activated carboxyl group from the biotin carboxylase domain to the carboxyl transferase domain, followed by carboxyl transfer to malonyl-CoA. Despite the intensive research on this enzyme, only the bacterial and yeast ACC structures are currently available, To explore the mechanism of ACC holoenzyme function, we determined the structure of the biotinoyl domain of human ACC2 and analyze its characteristics using NMR spectroscopy. The 3D structure of the hACC2 biotinoyl domain has a similar folding topology to the previously determined domains from E. coli and P. Shermanii, however, the 'thumb' structure is absent in the hACC2 biotinoyl domain. Observations of the NMR signals upon the biotinylation indicate that the biotin group of hACC2 does not affect the structure of the biotinoyl domain, while the biotin group for E. coli ACC interacts directly with the thumb residues that are not present in the hACC2 structure. These results imply that, in the E. coli ACC reaction, the biotin moiety carrying the carboxyl group from BC to CT can pause at the thumb of the BCCP domain. The human biotinoyl domain, however, lacks the thumb structure and does not have additional non-covalent interactions with the biotin moiety; thus, the flexible motion of the biotinylated lysine residue must underlie the "swinging arm" motion. This study provides insight into the mechanism of ACC holoenzyme function and supports the "swinging arm" model in human ACCs.

Curie Temperature and Tunable Dielectric Properties of Barium Strontium Titanate Thick Films (티탄산 바륨 스트론튬 (BaxSr1-xTiO3) 후막의 상전이온도와 가변 유전특성)

  • Jeon, So-Hyun;Kim, In-Sung;Min, Bok-Ki;Song, Jae-Sung;Yoon, Jon-Do
    • Journal of the Korean Ceramic Society
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    • v.43 no.7 s.290
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    • pp.421-426
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    • 2006
  • [ $(BaSr)TiO_3$ ] thick films were prepared by tape casting method, using $BaTiO_3\;and\;SrTiO_3$ powder slurry in order to investigate dielectric properties i.e. dielectric constant, ${\varepsilon}_r$, Curie temperature, $T_c$. Grain growth within $(BaSr)TiO_3$ thick films was observed with increasing weight ratio of $BaTiO_3$. This observation can be explained by phenomena of substitution of $Sr^{2+}$ ion for $Bi^{2+}$ ion in the $BaTiO_3$ system. Also, the Curie temperature in $(BaSr)TiO_3$ thick films was shifted to lower temperature range with increasing $ SrTiO_3$. Furthermore, Curie temperature having maximum dielectric constant was in the range of $-40^{\circ}C\;to\;30^{\circ}C$, and hence sharper phase transformation occurred at Curie temperature. There occurred decrease in tunability and k-factor of $(Ba_{0.6}Sr_{0.4})TiO_3$ calculated from the dielectric constant, ${\varepsilon}_r$ above Curie temperature. In addition, above the $60^{\circ}C$, phase fixation was observed. This means that internal stress relief occurred with increasing $90^{\circ}$ domains.

Cloning, Purification and NMR Studies on β-catenin C-terminal Domain

  • Oh, Jeongmin;Choi, Sooho;Yun, Ji-Hye;Ko, Yoon-Joo;Choi, Kang-Yell;Lee, Weontae
    • Journal of the Korean Magnetic Resonance Society
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    • v.21 no.2
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    • pp.72-77
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    • 2017
  • ${\beta}-catenin$ is a key signaling protein which regulates cell signaling and gene transcription. Abnormal activation of ${\beta}-catenin$ is linked to many cancers, particularly with colorectal cancers. Although many genetic and biological studies on $Wnt/{\beta}-catenin$ have been reported and structures of the complex between ${\beta}-catenin$ and its diverse binding partners have been published, many of them have focused on armadillo repeat domain of ${\beta}-catenin$. Both N- and C-terminal domains have been suggested to regulate interactions of ${\beta}-catenin$ with other molecules, but still little is known about the C-terminal unstructured domain. To investigate the structure of this domain, construct of C-terminus was designed and structural studies were performed using size exclusion chromatography (SEC), circular dichroism (CD), fluorescence and nuclear magnetic resonance (NMR) spectroscopy. We observed that not only the purified full-length construct but the purified C-terminal construct also dimerizes in solution by SEC, suggesting that this domain involves in dimerization of ${\beta}-catenin$. CD and fluorescence data indicate its flexibility and structural formation in the presence of membrane environments.

Secondary Structure, 1H, 13C and 15N Resonance Assignments and Molecular Interactions of the Dishevelled DIX Domain

  • Capelluto, Daniel G.S.;Overduin, Michael
    • BMB Reports
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    • v.38 no.2
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    • pp.243-247
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    • 2005
  • Dishevelled (Dvl) is a positive regulator of the canonical Wnt signaling pathway, which regulates the levels of $\beta$-catenin. The $\beta$-catenin oncoprotein depends upon the association of Dvl and Axin proteins through their DIX domains, and its accumulation directs the expression of specific developmental-related genes at the nucleus. Here, the $^1H$, $^{13}C$, and $^{15}N$ resonances of the human Dishevelled 2 DIX domain are assigned using heteronuclear nuclear magnetic resonance (NMR) spectroscopy. In addition, helical and extended elements are identified based on the NMR data. The results establish a structural context for characterizing the actin and phospholipid interactions and binding sites of this novel domain, and provide insights into its role in protein localization to stress fibers and cytoplasmic vesicles during Wnt signaling.

Vibration Control of a Passenger Vehicle Featuring MR Suspension Units (MR 현가장치를 장착한 승용 차량의 진동제어)

  • 이환수;최승복;이순규
    • Journal of KSNVE
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    • v.11 no.1
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    • pp.41-48
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    • 2001
  • This paper presents vibration control performance of a passenger vehicle featuring magneto-rheological (MR) suspension units. As a first step, a cylindrical shock absorber is designed and manufactured on the basis of Bingham Property of a commercially available MR fluid. After verifying that the damping force of the shock absorber can be controlled by the intensity of magnetic field(or input current), it is applied to a full-car model. An optimal controller is then formulated to effectively suppress unwanted vibration of the vehicle system. The control performances are evaluated via hardware-in-the-loop simulation(HILS), and presented in both time and frequency domains.

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