• Bulletin of the Korean Chemical Society
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• 제26권7호
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• pp.1051-1056
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• 2005

The interaction of bovine carbonic anhydrase II with copper ions was studied by isothermal titration microcalorimetry, circular dichroism, UV spectrophotometry and temperature scanning spectrophotometry methods at 27 ${^{\circ}C}$ in Tris buffer solution at pH = 7.5. It was indicated that there are three non-identical different binding sites on carbonic anhydrase for $Cu^{2+}$. The binding of copper ions is exothermic and can induce some minor changes in the secondary and tertiary structure of the enzyme, which does not unfold it, but can result in a decrease in both activity and stability of the enzyme.

• Bulletin of the Korean Chemical Society
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• 제30권2호
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• pp.415-418
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• 2009

Concerned with ambiguous stereochemistry assignment of natural (+)-glabridin, absolute configurations of (${\pm}$)-glabridin enantiomers were studied with synthetic glabridin. Synthetic glabridin enantiomers were separated by semi-preparative Sumi-chiral column chromatography, and characterized by UV-Vis and NMR spectroscopy. Three-dimensional molecular structure of glabridin was obtained as equatorial Ph-3 half chair chroman ring from semi-empirical PM3 calculation, and refined by coupling constants in $^1H$ NMR spectrum. Finally, absolute configurations of two enantiomers were determined by circular dichroism spectroscopy based on the empirical helicity rules. Absolute configuration of natural (+)-glabridin was confirmed as (R)-glabridin, as known.

• 한국자기학회:학술대회 개요집
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• 한국자기학회 2000년도 International Symposium on Magnetics The 2000 Fall Conference
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• pp.207-216
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• 2000

Soft x-ray standing waves produced by a multilayer interference substrate add depth-sensitivity to magnetic circular dichroism to resolve changes in Co magnetism across a 10 ${\AA}$ distance from the Co center to the Co-Pd interface of a Pd/Co/Pd trilayer having in-plane magnetization. Large enhancements of in-plane orbital and spin magnetic moments, as well as the number of d holes, are strongly localized in thin interface layer. These results provide new insight into the phenomenon of magnetic anisotropy at buried interfaces, and suggest a broad applicability of such standing wave measurements to interface magnetism studies.

• 한국자기공명학회논문지
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• 제12권1호
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• pp.40-50
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• 2008

Ghrelin is a unique peptide hormone that releases growth factor and it stimulates appetite. It comes from pre pro-ghrelin by the post translational modification process and its innate functions are known as food up-take and the growth hormone regulation. Therefore, the structural information of ghrelin precursor is of importance in understanding it function. From our results, we found that the solution structure of ghrelin is mostly random coil conformation at neutral pH value and the structural population changes with pH environments. Data from circular dichroism in different TFE concentrations revealed that the secondary structure changes from random coil to a-helix and the isodichroic point is observed at 202nm, implying that two equilibrium states exist between random coil and helical structure.

• Journal of Photoscience
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• 제12권1호
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• pp.11-15
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• 2005

The mechanism of interaction of two drugs viz., amoxicillin and cloxacillin with bovine serum albumin has been investigated using fluorescence absorption and circular dichroism spectroscopy. The quenching mechanism of fluorescence of bovine serum albumin by amoxicillin and cloxacillin was discussed. The binding sites number n and apparent binding constant Kwere measured by fluorescence quenching method. The thermodynamic parameters obtained from data at different temperatures were calculated. The distance r between donor (bovine serum albumin) and acceptor (amoxicillin and cloxacillin) was obtained according to Forster theory of non-radiative energy transfer. The effect of common ions on binding constant was also investigated. The results of synchronous fluorescence spectra, UV-vis absorption spectra and circular dichroism of BSA in presence of amoxicillin and cloxacillin show that the conformation of bovine serum albumin changed

• Bulletin of the Korean Chemical Society
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• 제6권4호
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• pp.214-217
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• 1985

Platinum(II) complexes of R-2,2'-diaminobinaphthyl (R-dabn), [Pt(R-dabn)(H2O)2]Cl2, [Pt(R-dabn)(R-Pn)]Cl2, [Pt(R-dabn)(R-bn)]Cl2, and platinum(II) complexes of S-2,2'-diaminobinaphthyl (S-dabn), [Pt(S-dabn)(H2O)2]Cl2, [Pt(S-dabn)(S-Pn)]Cl2, and [(Pt(S-dabn)(S-bn)]Cl2 have been prepared. (R-Pn and S-Pn are, respectively R- and S isomer of 2,3-diaminobutane). R-Pn and S-bn are, respectively R and S isomer of 2,3-diaminopropane). In the vicinity of the B-absorption band region of dabn, the circular dichroism spectra of platinum(Ⅱ) complexes of R-dabn series show a positive B-band followed by a negative higher energy A-band, which is generally understood as the splitting pattern for a ${\lambda}$ conformation, while the circular dichroism spectra of platinum(Ⅱ) complexes of S-dabn series show a negative B-band followed by a positive higher energy A-band in the long-axis polarized absorption region as expected for a $\delta$ conformation.

• 한국진공학회:학술대회논문집
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• 한국진공학회 2005년도 제28회 학술발표회 초록집
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• pp.42-42
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• 2005

• Bulletin of the Korean Chemical Society
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• 제28권6호
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• pp.1063-1066
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• 2007

• 한국식품영양학회지
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• 제15권4호
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• pp.331-336
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• 2002

본 연구는 두유에 칼슘을 강화하고자 두유단백질의 칼슘내인성을 높이기 위한 방법으로 단백분해효소를 처리한 경우 효소처리 전, 후에 나타나는 단백질의 구조적 특성을 비교 분석하였다. 표면소수도는 SMP

• Applied Biological Chemistry
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• 제51권4호
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• pp.276-280
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• 2008

식품 allergen 저감화 수단으로 자외선 조사의 타당성을 검토하고 자외선조사가 식품 단백질의 분자적 성질에 미치는 영향을 조사하고자 ovalbumin 용액에 자외선을 조사한 후 단백질의 분자량 분포와 2차구조 및 3차구조의 변화를 조사하였다. SDS-PAGE와 Gel permeation chromatography 결과 ovalbumin은 자외선 조사에 의하여 단백질이 분해되고 조사시간이 증가할수록 펩티드가 중합하는 형태를 나타냈다. Circular dichroism 연구는 자외선 조사에 의하여 ${\alpha}$-helix 구조가 감소하고 조사시간이 증가할 경우 compact denatured ovalbumin의 구조를 나타내는 2차구조의 변화를 나타냈다. 자외선 조사된 ovalbumin의 형광스펙트럼은 조사시간이 증가할수록 단백질의 maximum emission intensity가 감소하는 3차구조의 변화를 나타냈다. 결과적으로 자외선 조사는 ovalbumin의 분자적 성질을 변화시키며 allergen의 항원성을 변화시키는 수단으로 이용가능성을 시사한다.