• Journal of Pharmaceutical Investigation
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• v.22 no.3
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• pp.237-240
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• 1992

A series of biodegradable block copolymers consisting of $poly({\gamma}-benzyl\;L-glutamate)$ (PBLG) and poly(ethylene oxide) (PEO)-lactoselactone were prepared by polymerization of PEO-lactoselactone and ${\gamma}-benzyl$ L-glutamate-N-carboxyanhydride and characterized by IR and NMR. From circular dichroism measurements, it was found that the polymers exist in the ${\alpha}-helical$ conformation. Block copolymer microspheres were prepared by solvent-extraction-precipitation method for their primary evaluation for medical and biological applications.

• Proceedings of the Korean Society of Postharvest Science and Technology of Agricultural Products Conference
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• 2003.10a
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• pp.135.1-135
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• 2003

To elucidate the effect of gamma-irradiation on the molecular properties of hemoglobin, the secondary, tertiary structure, and the molecular weight size of the protein were examined after irradiation at 0.5, 1, 5, and 10 kGy. Gamma-irradiation of hemoglobin solutions caused the disruption of the ordered structure of the protein molecules, as well as degradation, cross-linking, and aggregation of the polypeptide chains. A SDS-PAGE study indicated that irradiation caused initial fragmentation of the proteins and subsequent aggregation due to cross-linking of the protein molecules. The effect of irradiation on the protein was more significant at lower protein concentrations. Ascorbic acid decreased the degradation and aggregation of proteins by scavenging oxygen radicals that were produced by irradiation. A circular dichroism study showed that irradiation decreased the helical content of hemoglobin with a concurrent increase of the aperiodic structure content. Fluorescence spectroscopy indicated that irradiation decreased the emission intensity that was excited at 280 nm.

• Bulletin of the Korean Chemical Society
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• v.29 no.9
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• pp.1839-1842
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• 2008

• Proceedings of the Korean Biophysical Society Conference
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• 1999.06a
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• pp.18-18
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• 1999

A sweet protein monellin was originally isolated from the berries of the West African plant Dioscoreophyllum cumminsii. The studies for molecular interaction of different sweeteners with receptor as well as receptor binding model have been proposed previously. The high-resolution solution structure of single-chain monellin (SCM) has been determined to investigate structural origin of sweet taste by NMR spectroscopy and simulated annealing calculations.(omitted)

• Journal of the Korean Magnetics Society
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• v.5 no.4
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• pp.309-314
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• 1995

최근 새로운 과학기술의 발달로 자기다층박막등 자기 분야의 신소재를 비롯하여 XMCD( X-ray Magnetic Circular Dichroism), MFM(Magnetic Force Microscope)등 자성분석방법등이 개발되고 있고, 정보화 사회의 출현과 함께 자기기록에 대한 중요성이 증대되면서 자기 물성에 대한 연구는 새로운 르네상스 시기를 맞았다고 할 수 있다. 자기 현상의 근본 원리 규명에 대한 연구는 재료과학 또는 고체물성 연구과제중 가장 오랜 역사를 지닌 문제중의 하나라 할 수 있다. 자연계에 존재하는 자석은 기원전 7세기경부터 인간에게 알려진 것으로 기록되어 있고 그후 오랫동안 나침반으로 사용되어 왔다. 하지만 자석의 원리에 대한 규명은 양자역학이 생기고 전자의 스핀개념이 도입된 20세기 초에서야 시작되어졌다. 그나마 현재까지도 자기현상의 아주 기본적인 개념만이 알려진 상황이고, 금속, 부도체 또는 화합물등에서 일어나는 다양한 자기 현상들을 일관성 있게 설명하는 완전한 이론의 정립은 아직도 요원한 문제라 할 수 있다.

• Archives of Pharmacal Research
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• v.10 no.2
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• pp.110-114
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• 1987

To correlate the conformational changes of DNA (Calf Thymus) with entrapment of DNA into liposomes, the effect of ions ($Na^+$, $Mg^{++}$on the entrapment of calf thymus DNA into liposomes was investigated. The effect of divalent ion ($Mg^{++}$ on the structural changes of DNA indicated by decrease of observed ellipticity at 274 nm and nonspecific binding of DNA to lipid bilayers was greater than monovalent ion ($\Na^+$). But the efficiency of DNA encapsulated was not altered. These results show that entrapment of DNA into liposomes is not due to nonspecific binding and structural changes because of electrostatic forces but to mechanical capture of DNA by the internal aqueous space of liposomes although divalent ion contributes large structural changes and more nonspecific association of DNA with liposomes due to strong charges.

• Archives of Pharmacal Research
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• v.4 no.2
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• pp.99-107
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• 1981

To investigate the protein binding characteristics of ibuprofenlysine, the effects of drub conentration, pH, ionic strength and protein concentration on the binding of drug to protein concentration on the binding of drug to protein were studied by fluorescence probe method. The conformational change of protein was investigated by circular dichroism (CD) measurement. As the concentration of drug increases, the association constant decreases. These may be due to complex formation of the probe and drug, or the interaction of the protein-probe complex and drug. The association constant for ibuprofenlysine increased with increasing protein concentration. These finding suggest a sharing of one ibuprofenlysine molecule by more than one protein molecule in the binding. The binding between ibuprofenlysine and protein was dependent on pH and ionic strength. It seems that both hydrophobic binding and some electrostatic forces are involved in the binding of ibuprofenlysing to protein.

• Proceedings of the Korean Vacuum Society Conference
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• 2010.02a
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• pp.378-378
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• 2010

We report the electronic structure of CoFeO-R (R=Hf, La, Nb) thin films studied by x-ray absorption spectroscopy (XAS). These ferrites thin films were prepared by pulsed laser deposition method and characterized by XAS measurements at O K-, Co and Fe L-edges. The O K-edge spectra suggest that there is a strong hybridization between O 2p and 3d electrons of transition metal cations and Fe $L_{3,2}$-edge spectra indicate that Fe-ions exist in $Fe^{2+}$ with tetrahedral site of the spinel structure. Divalent Co ions is also distributed in tetrahedral site with rare earth ions goes to octahedral sites of spinel structure. X-ray magnetic circular dichroism (XMCD) is also used to explain the symmetry and magnetic nature dependence on rare-earth ions.

• Bulletin of the Korean Chemical Society
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• v.16 no.1
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• pp.42-47
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• 1995

Interpolymer complex formation between basic polypeptide poly(L-proline) Form Ⅱ (PLP(Ⅱ)) and acidic polypeptides poly(L-glutamic acid) (PLGA) and poly(L-aspartic acid)(PLAA) has been studied in water-methanol (1:2 v/v) mixed-solvent by viscometry, potentiometry, light scattering and circular dichroism (CD) measurements. It has been found that polymer complexes between PLP(Ⅱ) and PLGA (or PLAA) are formed via hydrogen bonding with a stoichiometric ratio of PLP(Ⅱ)/PLGA (or PLAA)=1:2 (in unit mole ratio) and that PLP(Ⅱ) forms polymer complex more favorably with PLGA than with PLAA. In addition, the minimum (for pH 5.0) and the maximum (for pH 3.2) in reduced viscosity of dilute PLP(Ⅱ)-PLGA mixed solutions are observed at 0.67 unit mole fraction of PLGA (i.e., [PLP(Ⅱ)]/[PLGA]=1/2). These findings could be explained in terms of molecular structure (or conformation) of the complementary polymers associated with the complex formation.

• Bulletin of the Korean Chemical Society
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• v.18 no.1
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• pp.50-56
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• 1997

The mode of action of mastoparan B, an antimicrobial cationic tetradecapeptide amide isolated from the hornet Vespa basalis, toward phospholipid bilayers was studied with synthetic mastoparan B and its analogs with individual Ala instead of hydrophobic amino acids (1-Ile, 3-Leu, 6-Leu, 7-Val, 9-Trp, 13-Val, 14-Leu) in mastoparan B. Mastoparan B and its analogs were synthesized by the solid-phase method. Circular dichroism spectra showed that mastoparan B and its analogs adopted an unordered structure in buffer solution. In the presence of neutral and acidic liposomes, most of the peptides took an α-helical structure. The calcein leakage experiment indicated that mastoparan B interacted strongly with neutral and acidic lipid bilayers than its analogs. Mastoparan B also showed a more or less highly antimicrobial activity and hemolytic activity for human erythrocytes than its analogs. These results indicate that the hydrophobic face in the amphipathic α-helix of mastoparan B critically affect biological activity and helical contents.