• Proceedings of the Korean Society of Potoscience Conference
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• spring
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• pp.89-90
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• 1999

• Journal of the Korean Magnetic Resonance Society
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• v.22 no.1
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• pp.18-25
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• 2018

Replication protein A (RPA) is an essential single-stranded DNA binding protein in DNA processing. It is known that N terminal domain of RPA70 (RPA70N) recruits various protein partners including damage-response proteins such as p53, ATRIP, Rad9, and MRE11. Although the common binding residues of RPA70N were revealed, dynamic properties of the protein are not studied yet. In this study, we measured $^{15}N$ relaxation parameters ($T_1,\;T_2$ and heteronuclear NOE) of human RPA70N and analyzed them using model-free analysis. Our data showed that the two loops near the binding site experience fast time scale motion while the binding site does not. It suggests that the protein binding surface of RPA70N is mostly rigid for minimizing entropy cost of binding and the loops can experience conformational changes.

• Journal of the Korean Magnetic Resonance Society
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• v.6 no.1
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• pp.1-11
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• 2002

Physical properties of PVB [Poly(vinyl butyral)] polymer are strongly correlated with water contents in the polymer. Thus dynamics of PVB containing 10~50(w/w) ％ of water were studied by $^{13}$ C CP/MAS/DD over the temperature range 293K -348K. From the Peak area, line width, chemical shift, and relaxation times ( $T_{1}$ $T_{1p}$) measured at 9.4 T, it was deduced that water facilitates molecular dynamics of the PVB molecules overall including conformational exchange of the racemic and meso butyaldehyde rings in the PVB. However, the influence of water was not linear to the amount of water in the PVB samples. It is suggested that water up to 30 w/w ％ of the sample is closely bound to the PVB polymer and water relatively free from the PVB polymer starts to appear when water is added more than 30 w/w ％.％.

• Bulletin of the Korean Chemical Society
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• v.18 no.4
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• pp.415-424
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• 1997

Conformational flexibilities of the GlcNAc(β1,3)Gal(β)OMe are investigated through NMR spectroscopy and molecular modeling. Adiabatic energy map generated with a dielectric constant of 50 contains three local minima. All of the molecular dynamics simulations on three local minimum energy structures show fluctuations between two low energy structures, N2 at φ=80° and ψ=60° and N3 at φ=60° and ψ=-40°. We have presented adequate evidences to state that GlcNAc(β1,3)Gal(β)OMe exists in two conformationally discrete forms. Two state model of N2 and N3 conformers with a population ratio of 40:60 is used to calculate the effective cross relaxation rate and reproduces the experimental NOEs very well. Molecular dynamics simulation in conjunction with two state model proves successfully the dynamic equilibrium existed in GlcNAc(β1,3)Gal(β)OMe and can be considered as a powerful method to analyze the motional properties in the structure of carbohydrate. This observation also cautions against the indiscriminate use of a rigid model to analyze NMR data.

• Journal of the Korean Magnetic Resonance Society
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• v.28 no.3
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• pp.10-14
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• 2024

Caveolin3, mainly expressed in muscle tissue types, is a structural scaffolding protein of caveolae which are microdomains of plasma membrane. To elucidate the relationship between structure and function, several studies on the structure of caveolins using NMR have been reported. Because the ionic strength can affect the electrostatic-driven association of proteins with ligand and protein structure, the effect of salt in the structural studies has to be considered. In this work, we observed that the chemical shifts of Cav3 in the LPPG detergent change depending on salt concentration. The R2 values also show salt concentration-dependent changes. Specifically, in the N-terminal region where conformational changes and various interactions occur, the R2 values decrease. Interestingly, the R2 values of residues expected to be located in the LPPG detergent are also influenced by the salt concentration. This work suggests that the concentration of NaCl can affect interpretation of NMR data from membrane proteins.

• Macromolecular Research
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• v.17 no.4
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• pp.245-249
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• 2009

A fluorescing, copolymer(Q)-bearing, quaternary ammonium pendant was mixed with excess natural salmon sperm DNA with a molecular weight of $1.3{\times}10^6$(2,000 base pairs) to afford highly fluorescing, complex mixtures. The fluorescence life-time of the polymer Q was greatly increased when mixed with DNA: for the mixture of Q:DNA=1:750 the fast and slow decay lifetimes increased from ca. 10 to 100 ps and from 20 ps to ca. 1 ns, respectively. The enhanced fluorescence of the mixtures was ascribed to efficient compartmentalization and reduced conformational relaxation of the polymer Q by complexation with excess DNA.

• Bulletin of the Korean Chemical Society
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• v.30 no.4
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• pp.849-852
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• 2009

The work describes EPR and 17O NMR measurements followed by theoretical calculation of the rotational correlation time $({\tau}_R)$, the water residence time $({\tau}_m)$, and the longitudinal electronic spin relaxation time $(T_{le})$(T_1e) for two new gadolinium complexes 1 and 2 of the type [$Gd(L)(H_2O)$] (L = tranexamic esters) in order to investigate their efficiency as a paramagnetic contrast agent (PCA). Of three correlation times, τR plays a major and predominant role to the unusually high relaxivity of 1 and 2 as compared with that of clinically approved MR CAs such as [$Gd(DTPA)(H_2O)]2‐ (Magnevist${\circledR}$), [Gd(DTPA-BMA)(H2O)] (Omniscan${\circledR}$), and $[Gd(DOTA)(H_2O)]^-$ (Dotarem${\circledR}$). The presence of bulky tranexamic ester in the ligand seems to be responsible for the conformational rigidity, which in turn causes such great an increase in ${\tau}_R$.

• The Korean Journal of Physiology and Pharmacology
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• v.5 no.5
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• pp.397-405
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• 2001

The ryanodine receptor, a $Ca^{2+}$ release channel of the sarcoplasmic reticulum (SR), is responsible for the rapid release of $Ca^{2+}$ that activates cardiac muscle contraction. In the excitation-contraction coupling cascade, activation of SR $Ca^{2+}$ release channel is initiated by the activity of sarcolemmal $Ca^{2+}$ channels, the dihydropyridine receptors. Previous study showed that the relaxation defect of diabetic heart was due to the changes of the expressional levels of SR $Ca^{2+}$ATPase and phospholamban. In the diabetic heart contractile abnormalities were also observed, and one of the mechanisms for these changes could include alterations in the expression and/or activity levels of various $Ca^{2+}$ regulatory proteins involving cardiac contraction. In the present study, underlying mechanisms for the functional derangement of the diabetic cardiomyopathy were investigated with respect to ryanodine receptor, and dihydropyridine receptor at the transcriptional and translational levels. Quantitative changes of ryanodine receptors and the dihydropyridine receptors, and the functional consequences of those changes in diabetic heart were investigated. The levels of protein and mRNA of the ryanodine receptor in diabetic rats were comparable to these of the control. However, the binding capacity of ryanodine was significantly decreased in diabetic rat hearts. Furthermore, the reduction in the binding capacity of ryanodine receptor was completely restored by insulin. This result suggests that there were no transcriptional and translational changes but functional changes, such as conformational changes of the $Ca^{2+}$ release channel, which might be regulated by insulin. The protein level of the dihydropyridine receptor and the binding capacity of nitrendipine in the sarcolemmal membranes of diabetic rats were not different as compared to these of the control. In conclusion, in diabetic hearts, $Ca^{2+}$ release processes are impaired, which are likely to lead to functional derangement of contraction of heart. This dysregulation of intracellular $Ca^{2+}$ concentration could explain for clinical findings of diabetic cardiomyopathy and provide the scientific basis for more effective treatments of diabetic patients. In view of these results, insulin may be involved in the control of intracellular $Ca^{2+}$ in the cardiomyocyte via unknown mechanism, which needs further study.