• Title/Summary/Keyword: Conformation in solution

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The Gelation Studies of PAA Polyelectrolytes in Aqueous Media (폴리 아크릴산 고분자전해질의 수용액 속에서의 겔화에 관한 연구)

  • Sohn, Jeong-In
    • Applied Chemistry for Engineering
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    • v.5 no.3
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    • pp.443-450
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    • 1994
  • Polyelectrolytes of various ionization degrees, which are prepared by neutralization of poly(acrylic acid)(PAA), were crosslinked by ethylane glycol diglycidyl ether(EGDE) in aqueous solution. $C_{gel}$, the minimum polymer concentration at which gelation occurs, was higher than expected. $C_{gel}$ was comparable with that of neutral polymer. This is considered to be due to the size contraction of polyelectrolyte, which comes from ionic strength increase as polymer concentration is increased. $C_{gel}$ is low when molecular weight of the sample becomes high. It reveals that polyelectrolyte is crosslinked in coil form not in extended rod form. This behavior is similar to the crosslinking of neutral polymers. Polyelectrolytes of partially ionized sample generally follow the behavior of fully ionized polyelectrolyte. Polyelectrolyte with added salt was also studied. Considering the pH dependence of EDGE reactivity it was difficult to compare the system which differs in pH significantly.

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Cryoprotective Effect and Mechanism of Corn Starch Enzyme Hydrolysates on Fish Protein 2. Cryoprotective Mechanism of Corn Starch Enzyme Hydrolysates on Fish Protein (전분가수분해물의 어육단백질 동결변성 방지효과 및 작용기구 2. 옥수수전분가수분해물의 어육단백질에 대한 동결변성 방지 기구)

  • LEE Kang-HO;JUNG Byung-Chun;HONG Byung-Il
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.31 no.6
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    • pp.829-834
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    • 1998
  • It is well known that the native conformation of many proteins can be stabilized by carbohydrates or polyalcohols. However, the mechanism of the stabilization still remains unclear. In the present studies, to characterize the cryoprotective mechanism of corn starch enzyme hydrolysates on fish protin, solubility of hydrolysates, thermal behavior of hydrolysates and actomyosin solution, and enzyme kinetics in frozen system were investigated. The solubility of the hydrolysates increased with the increase in D.E. value. The $T_g^{'}$ of the hydrolysates were linearly correlated with D.E. value and the T-g value of the hydrolysates (D.E. 5,10,15,20) were reported to be $-7.2^{\circ}C\;-8.8^{\circ}C\;-11.9^{\circ}C$, and $-14.3^{\circ}C$, respectively. The results of enzyme experiments showed that the higher the D.E. value, the higher was the rate of reaction in frozen storage ($-12^{\circ}C$). It is found to support the cryostabilization mechanism that the hydrolysats act to enmesh the protein in a glass state where all deteriorative processes are greatly slowed down.

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Elution Behavior of Protein and Pullulan in Asymmetrical Flow Field-flow Fractionation (AsFlFFF)

  • Ji, Eun-Sun;Choe, Seong-Ho;Yun, Guk-Ro;Chun, Jong-Han;Lee, Seung-Ho
    • Bulletin of the Korean Chemical Society
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    • v.27 no.9
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    • pp.1433-1438
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    • 2006
  • An AsFlFFF channel was designed and built, and then tested for analysis of pullulans and proteins. Pullulans and proteins having various nominal molecular weights were injected at various conditions of the cross-flow rate ($F_c$) and the channel-out flow rate ($F_{out}$). The retention (measured by the retention ratio R) and the zone broadening (measured by the plate height H) were measured, and then compared with theory. When the incoming flow rate, $f_{in}$ (and thus $F_{out}$) was varied with $F_c$ fixed at 2.5 mL/min, the plate height measured for the pullulan with nominal molecular weight (M) of about 100,000 showed the trend expected by the longitudinal diffusion theory (H decreases with increasing flow rate). In contrast, when $F_{out}$ was varied with the flow rate ratio, $F_c/F_{out}$, fixed constant at 5, the plate height measured for the same sample showed the trend expected from the non-equilibrium theory (H increases with increasing flow rate). Calibration plots (log D vs. log M) obtained with pullulans and proteins were not coincide, probably due to the difference in molecular conformation, suggesting the analysis of pullulans and proteins using AsFlFFF requires independent calibration. It was found that the linearity of the protein-calibration plot was improved by using a buffer solution as the carrier.

Structural and Molecular Characterization of Extracellular Polysaccharides Produced by a New Fungal Strain, Trichoderma erinaceum DG-312

  • JOO JI-HOON;YUN JONG-WON
    • Journal of Microbiology and Biotechnology
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    • v.15 no.6
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    • pp.1250-1257
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    • 2005
  • Two groups of exopolysaccharides (designated as Fr-I EPS and Fr-II EPS) were isolated from the culture filtrate of new fungal strain Trichoderma erinaceum DG-312 by Sepharose CL-6B chromatography. The structures of the exopolysaccharides were investigated using gas chromatography (GC), Fourier transform-infrared (FT-IR) spectroscopy, GCMS analysis, and NMR. GC analysis indicated that Fr-I EPS was composed of mainly mannose ($78.9\%$) and galactose ($21.1\%$), whereas Fr-II EPS contained mannose ($68.4\%$), galactose ($26.2\%$), and glucose ($5.4\%$). In the anomeric region ($950-700cm_{-1}$) of the FT-IR spectrum, both EPSs exhibited obvious characteristic absorption of $810\;cm_{-1}$, indicating the existence of mannose. The spectra of $\alpha-and\;\beta$-configurations were assigned at 880 and $914\;cm_{-1}$, respectively. The results of GC-MS analyses confirmed that both EPSs were complex heteropolysaccharides with a ($1{\rightarrow}3$)-linked mannan backbone. The C-1 region that appeared in the $^{13}C-NMR$ spectra of these EPSs indicated a typical anomeric carbon signal. The Fr-I EPS showed two anomeric carbon signals at 102.6 and 99.6 ppm, whereas the Fr-II EPS displayed four anomeric carbon signals at 102.5, 99.6, 98.5, and 94.3 ppm. The molecular characteristics of the EPSs were further investigated using a size exclusion chromatography/multi-angle laser light scattering (SEC/MALLS) system. The SEC/MALLS system revealed that the average molar masses of the EPSs were $6.592{\times}10^{4}$ (Fr-I EPS) and $1.920{\times}10^{4}$ (Fr-II EPS) g/mol, and the molecular conformation of both EPSs in aqueous solution was random coils.

Study on Relative Stability of Geometrically Constrained Cyclopropylcarbinyl Cation by $^{19}$F-NMR Spectroscopy (풀루오르 19-NMR을 이용한 구조적으로 고정된 사이크로프로필카르비닐 양이온의 상대적 안정도의 비교)

  • Jung Hyu Shin;Bo Hyeon Yoon
    • Journal of the Korean Chemical Society
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    • v.29 no.3
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    • pp.213-219
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    • 1985
  • The relative stability as a function of geometry in rigid cyclopropylcarbinyl cations was examined by $^{19}$F-nmr spectroscopy. 8-p-Fluorophenyl-tricyclo[3.3.1.0$^{2,7}$]octane-8-yl-(I), 9-p-fluorophenyl-tricyclo[3.3.1.0$^{2,8}$]nonane-9-yl (II), and 10-p-fluorophenyl-tricyclo[4.3.1.0$^{2,9}$]decane-10-yl cation(Ⅲ) were prepared from the corresponding carbinols in FSO$_3$H-SO$_2$ClF solution at -120$^{\circ}C$. $^{19}$F-nmr data indicate that the symmetrical bisected geometry of cyclopropane ring for ${\sigma}$-conjugation is a very impotant factor in charge delocalization. However, varied orientation of the bond angle ${\theta}$ within the bisected conformation does not affect the charge delocalization into the cyclopropane ring.

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Structural resemblance of the DNAJA-family protein, Tid1, to the DNAJB-family Hsp40

  • Jang, Jinhwa;Lee, Sung-Hee;Kang, Dong-Hoon;Sim, Dae-Won;Ryu, Kyung-Suk;Jo, Ku-Sung;Lee, Jinhyuk;Ryu, Hyojung;Kim, Eun-Hee;Won, Hyung-Sik;Kim, Ji-Hun
    • BMB Reports
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    • v.55 no.10
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    • pp.488-493
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    • 2022
  • The specific pair of heat shock protein 70 (Hsp70) and Hsp40 constitutes an essential molecular chaperone system involved in numerous cellular processes, including the proper folding/refolding and transport of proteins. Hsp40 family members are characterized by the presence of a conserved J-domain (JD) that functions as a co-chaperone of Hsp70. Tumorous imaginal disc 1 (Tid1) is a tumor suppressor protein belonging to the DNAJA3 subfamily of Hsp40 and functions as a co-chaperone of the mitochondrial Hsp70, mortalin. In this work, we performed nuclear magnetic resonance spectroscopy to determine the solution structure of JD and its interaction with the glycine/phenylalanine-rich region (GF-motif) of human Tid1. Notably, Tid1-JD, whose conformation was consistent with that of the DNAJB1 JD, appeared to stably interact with its subsequent GF-motif region. Collectively with our sequence analysis, the present results demonstrate that the functional and regulatory mode of Tid1 resembles that of the DNAJB1 subfamily members rather than DNAJA1 or DNAJA2 subfamily proteins. Therefore, it is suggested that an allosteric interaction between mortalin and Tid1 is involved in the mitochondrial Hsp70/Hsp40 chaperone system.

Comparison Study on Changes of Antigenicities of Egg Ovalbumin Irradiated by Electron Beam or X-Ray

  • Kim, Mi-Jung;Lee, Ju-Woon;Sung, Nak-Yoon;Kim, Su-Min;Hwang, Young-Jung;Kim, Jae-Hun;Song, Beom-Seok
    • Food Science of Animal Resources
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    • v.34 no.5
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    • pp.570-575
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    • 2014
  • This study was conducted to compare the effects of two forms of radiation (electron and X-ray; generated by an electron beam accelerator) on the conformation and antigenic properties of hen's egg albumin, ovalbumin (OVA), which was used as a model protein. OVA solutions (2.0 mg/mL) were individually irradiated by electron beam or X-ray at the absorbed doses of 0 (control), 2, 4, 6, 8, and 10 kGy. No differences between the two forms of radiation on the structural properties of OVA were shown by spectrometric and electrophoretic analyses. The turbidity of OVA solution increased and the main OVA bands on polyacrylamide gels disappeared after irradiation, regardless of the radiation source. In competitive indirect enzyme-linked immunosorbent assay, OVA samples irradiated by electron beam or X-ray showed different immunological responses in reactions with monoclonal and polyclonal antibodies (immunoglobulin G) produced against non-irradiated OVA. The results indicate that electron beam irradiation and X-ray irradiation produced different patterns of structural changes to the OVA molecule.

Preparation and Characterization of PEG-impregnated Aloe Gel through DIS Processing of Aloe vera Leaf Slice (DIS 공정에 의한 Polyethylene Glycol 함침 알로에 베라 겔의 제조 및 특성화)

  • Kwon, Hye Mi;Hur, Won;Lee, Shin Young
    • KSBB Journal
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    • v.28 no.6
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    • pp.356-365
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    • 2013
  • The novel Aloe gels were prepared with dewatering and impregnation by soaking (DIS) processing of Aloe vera leaf slice at four different temperatures (25, 35, 45 and $55^{\circ}C$), using dehydration solution of 40% (w/v) polyethylene glycol (PEG4000). The PEG-impregnation to Aloe vera leaf slice during DIS was observed depending on immersion temperature, and the PEG-impregnated Aloe vera gel (PEG-i-AVG) obtained was characterized using $^1H$ NMR, FT-IR, GPC, XRD and TGA. The PEG-i-AVG had the higher levels of Aloe bioactives (glucomannan and O-acetyl contents) and better quality indices by $^1H$ NMR and FT-IR spectroscopy than those of native Aloe gel. Also, the obtained Aloe gel maintained the bimodal patterns in higher molecular weight region by GPC indicating no degradation of polysaccharide from native Aloe gel. The result observed by SEM confirmed a surface modification by forming the porous structure, and TGA result exhibited better thermal stability than that of native Aloe gel. XRD result revealed that the crystalline structure in Aloe gel was led by incorporation of PEG. Significant decrease of %insolubility and high enhancement of water solubility index were observed, respectively, and highly ordered conformation such as a helix structure was also indicated by Congo red reaction. We concluded that the modification effect for enhancing function of native Aloe gel was successfully obtained by DIS process using PEG as a dehydrating agent. These results suggested that this DIS process had a high potential for developing a new minimally processed product from Aloe vera leaf.

Stereoselective Electron-Transfer Reaction between Optical Active Cobalt(III) Complex and Racemic Cobalt(II) Complex (광학활성 코발트 (III) 착물과 라세미-코발트(II) 착물간의 입체선택적 전자전달반응)

  • Dong-Jin Lee;Maeng-Jun Jung;Myung-Ki Doh
    • Journal of the Korean Chemical Society
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    • v.35 no.5
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    • pp.500-505
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    • 1991
  • The stereoselectivity on the electron-transfer reaction between optical active ${\bigwedge}$-[CO(EDDS)]- and conformationally restricted complex $[Co({\pm}chxn)_3]^{2+}$ has been examined in aqueous solution. The products are four conformational isomers $(lel_3,\;lel_2ob,\;lelob_2,\;and\;ob_3)$ of ${\bigwedge}$-[Co(chxn)$_3]^{3+}$ with optical purities of 22% e.e, 25% e.e, 11% e.e, and 10% e.e, respectively. The reaction between ${\bigwedge}$-[CO(EDDS)]- and $[Co({\pm}chxn)_3]^{2+}$ in DMSO produced lel3-${\Delta}$ and lel2ob-${\Delta}$-[Co(chxn)$_3]^{3+}$ whose optical purities are 100% e.e, and 75% e.e, respectively.

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NMR structural studies on Human CD99 Type I

  • Kim, Hai-Young;Kim, Young-Mee;Joon Shin;Shin, Young-Kee;Park, Seong-Hoe;Lee, Weontae
    • Proceedings of the Korean Biophysical Society Conference
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    • 2003.06a
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    • pp.69-69
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    • 2003
  • Human CD99 is a ubiquitous 32-kDa transmembrane protein encoded by the mic2 gene. The major cellular functions of CD99 protein are related to homotypic cell adhension, apoptosis, vesicular protein transport, and differentiation of thymocytes or T cells. Recently it has been reported that expression of a splice variant of CD99 transmembrane protein (Type I and Type II) increases invasive ability of human breast cancer cells. To understand structural basis for cellular functions of CD99 (Type I), we have initiated studies on hCD99$^{TMcytoI}$ and hCD99$^{cytoI}$ using circular dichroism (CD) and multi-dimensional NMR spectroscopy. CD spectrum of hCD99$^{TMcytoI}$ in the presence of 200mM DPC and CHAPS displayed an existence $\alpha$-helical conformation. The solution structure of hCD99$^{cytoI}$ determined by NMR is composed of one N-terminal $\alpha$-helix, $\alpha$A, two C-terminal short $\alpha$-helix segments, $\alpha$B and $\alpha$C. While $\alpha$A and $\alpha$B are connected by the long flexible loop, $\alpha$B and $\alpha$C connected by type III$\beta$-turn. Although it has been rarely figured out the correlation between structure and functional mechanism of hCD99$^{TMcytoI}$ and hCD99$^{cytoI}$, there is possibility of dimerization or oligomerization. In addition, the feasible mechanism of hCD99$^{cytoI}$ is that it could have intramolecular interaction between the N- and C- terminal domain through large flexible AB loop.

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