• BMB Reports
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• v.28 no.6
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• pp.546-551
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• 1995

The conformation studies of myelin P2 protein and two of its major peptides were carried out using circular dichroism and fluorescence spectroscopy in water and in lipid environments. Significant conformational changes occur when the protein or peptides were bound to gangliosides. Similar effects were also found in trifluoroethanol solutions. The conformational features of P2 protein and its major peptides were discussed in relation to the environmental changes and the disease-inducing effects.

• Journal of the Optical Society of Korea
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• v.18 no.4
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• pp.365-369
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• 2014

We present accurate analytical solutions of the lineshapes of birefringence (rotation) and dichroism (absorption) spectroscopy for a circular anisotropic medium composed of atoms of the transition $J_g=0{\rightarrow}J_e=1$. The susceptibility of a weak probe beam was analytically calculated and was averaged over a Maxwell-Boltzmann velocity distribution. The lineshapes of the two spectroscopies were then presented in analytical forms at arbitrary values of the linewidths of the inhomogeneous (Doppler) broadening and the homogeneous (natural) broadening of the atoms.

• Journal of Magnetics
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• v.13 no.3
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• pp.85-87
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• 2008

I report a simple method to correct the saturation effect in absorption spectra measured in total electron yield (TEY) mode. It does not require additional measurements of the X-ray penetration depth. In order to check the reliability of the method, X-ray magnetic circular dichroism (XMCD) spectra for polycrystalline Fe were measured at two different incident angles, and then processed with the method. The two resultant XMCD spectra were identical, and their sum rule analysis produced the ratios of orbital magnetic moment to spin magnetic moment, which were very close to the well-known value.

• Journal of the Korean Magnetics Society
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• v.20 no.5
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• pp.201-205
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• 2010

X-ray magnetic circular dichroism (XMCD) has been used as an important tool of magnetics due to its unique abilities to measure element-specific magnetic properties and to separate the orbital and the spin magnetic moments. These abilities allow researchers to access the microscopic origin of the magnetic properties of transition metal and rare earth compounds. In this report, I explain the principle of XMCD and the experimental set-up. Recent a few research examples using XMCD will be also introduced.

• Bulletin of the Korean Chemical Society
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• v.30 no.2
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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.

• Journal of Photoscience
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• v.12 no.1
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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

• Applied Chemistry for Engineering
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• v.23 no.6
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• pp.577-582
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• 2012

In this work, vibrational circular dichroism (VCD) technique was applied for the determination of %EE of chiral compounds. It may provide an easy way to determine the %EE with a proper accuracy within 2% error ranges as well as the absolute configuration of enantiomers. We demonstrated herein a flow cell VCD (FT-VCD) technique for time-dependent %EE measurements. The simultaneous monitoring of the mole fraction and %EE for two chiral species (epichlorohydrin and glycidol mixture) in the mixture was shown to be successful without any further separation steps. Thus, we demonstrate that FT-VCD is an appropriate analytical tool to monitor the kinetics of reactions involving chiral molecules. FT-VCD also provides a convenient nondestructive approach for the time dependent determination of the optical purity of individual components in a reaction mixture containing chiral molecules.

• Proceedings of the Korean Magnetic Resonance Society Conference
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• 2000.01a
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• pp.28-28
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• 2000

• Journal of Applied Biological Chemistry
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• v.51 no.1
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• pp.17-19
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• 2008

Isoflavanone has been synthesized from the reduction of isoflavone in nearly quantitative yield. Isoflavone with seven equivalents of ammonium formate in the presence of Pd/C in ethanol under $N_2$ atmosphere exclusively produced the two-electron reduced product in two hours. It was characterized by various spectroscopic methods, including UV-VIS, EI-MS, $^1H$-NMR, $^{13}C$-NMR and $^1H$, $^1H$-COSY. The racemic mixture was separated by Sumi-Chiral column chromatography and the absolute configurations of the enantiomers were characterized by circular dichroism spectroscopy.

• Journal of the Korean Magnetic Resonance Society
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• v.13 no.1
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• pp.56-63
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• 2009

SWIRM domain, a core domain of SRG3 is well conserved in SW13, RSC8, and MOIRA family proteins. To understand structural basis for cellular functions of the SWIRM domain, we have initiated biochemical and structural studies on SWIRM domain and mutants using gelfiltration chromatography, circular dichroism and NMR spectroscopy. The structural properties of the mutant SWIRM domains (K34A and M75A) have been characterized, showing that the structures of both wild-type and mutant proteins are a-helical conformation. The data conclude that mutations at interaction sites of its binding partner protein do not affect its secondary and tertiary structure.