• Bulletin of the Korean Chemical Society
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• v.1 no.4
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• pp.117-121
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• 1980

The effect of lateral intermolecular interactions among the adsorbate molecules has been incorporated into the theory of multilayer physical adsorption developed previously by the present authors within the frame of Bragg-Williams approximation and the resulting adsorption isotherm has been used to interpret the adsorption data of tetramethylsilane vapor on clean iron film which we failed to account for in our previous works. The result has shown that up to the point where the relative pressure is about 0.7 considerable improvement is obtained but beyond this point there still remains large difference between theoretical and experimental isotherm. Such difference is supposed to arise from the neglect of effect of vertical interaction between the adsorbate molecules and the adsorbent surface.

• Archives of Pharmacal Research
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• v.13 no.3
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• pp.246-251
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• 1990

Intermolecular interaction between barbiturates and membrane components such as phospholipid and cholesterol were investigated on $^1$H-NMR spectra and infrared spectra. According to previous reports, barbiturates interacted with phospholipid through intermolecular hydrogen bonds. We also investigated thi observation using dipalmitoyl-phosphatidylcholine (DPPC) as phospholipid in deuterochloroform, and characterized quantitatively. Also, the observed drug could interact with cholesterol which is one of the major components of biomembranes through hydrogen bonds. It was the carbonyl groups of barbiturate and the hydroxyl group of cholesterol that formed hydrogen bond complex. In addition to spectroscopic studies, we investigated the direct effect of phenobarbital on lipid multibilayer vesicles, whose compositions were varied, by calorimetric method. Phenobarbital caused a reduction in the temperature of phase transition of vesicles. These studies may provided a basis for interpreting the mode of action of barbiturates.

• Journal of the Korean Magnetic Resonance Society
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• v.23 no.1
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• pp.33-39
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• 2019

Studies on the interactions of proteins with partner molecules at the atomic resolution are essential for understanding the biological function of proteins in cells and for developing drug molecules. Solution NMR spectroscopy has shown remarkably useful capability for investigating properties on the weak to strong intermolecular interactions in both diluted and crowded solution such as cell lysates. Of note, the state-of-the-art in-cell NMR method has made it possible to obtain atomistic information on natures of intermolecular interactions between target proteins with partner molecules in living cells. In this mini-review, we comprehensively describe the several technological advances and developments in the in-cell NMR spectroscopy.

• Proceedings of the Korean Institute of Electrical and Electronic Material Engineers Conference
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• 2009.04b
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• pp.97-98
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• 2009

Here, we describe a versatile strategy for precise control of the optoelectrical properties of the single walled carbon nanotube (SWNT)/silane binder hybrid films by noncovalent hybridization. Stable SWNT/silane binder solutions were prepared by direct mixing of high concentration CNT solutions and silane sol solutions. The critical binder content was determined by varying the amount of binder in the SWNT/binder solutions. A binder content of 50 wt% was used to prepare the other SWNT/binder solutions. This study demonstrates how the intermolecular interactions between the SWNTs and the silanes can affect the conductivity of the CNT/binder network films by characterizing the optoelectrical and Raman spectroscopic properties of the SWNT/silane films containing silane binders with various functional groups. The use of the PTMS binder with phenyl groups was found to be most effective in the fabrication of transparent and conductive films on glass substrates. Such a precise control of the optoelectrical properties of SWNT/binder films can be useful to fabricate the high performance conductive thin films, with ramifications for understanding the fundamental intermolecular interaction in carbon materials science.

• Proceedings of the Korean Fiber Society Conference
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• 2001.04a
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• pp.305-308
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• 2001

• Bulletin of the Korean Chemical Society
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• v.29 no.9
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• pp.1711-1716
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• 2008

The reaction of copper(II) chloride with phenyl-N-[(pyridine-2-yl)methylene]methaneamide (ppmma) leads to a new $\mu$ -chloro bridged dimeric [Cu(ppmma)$Cl_2$]$_2$ complex, whereas a reaction of copper(II) bromide with ppmma affords a monomeric Cu(ppmma)$Br_2$ complex. Both complexes have been characterized by X-ray crystallography and electronic absorption spectroscopy. The crystal structural analysis of [Cu(ppmma)$Cl_2$]$_2$ shows that the two Cu(II) atoms are bridged by two chloride ligands, forming a dimeric copper(II) complex and the copper ion has a distorted square-pyramidal geometry ($\tau$ = 0.2). The dimer units are held through a strong intermolecular $\pi-\pi$ interactions between the nearest benzyl rings. On the other hand, Cu(ppmma)Br2 displayed a distorted square planar geometry with two types of strong intermolecular π-π interaction. EPR spectrum of [Cu(ppmma)$Cl_2$]$_2$ in frozen glas s at 77 K revealed an equilibrium between the mononuclear and binuclear species. The magnetic susceptibilities data of [Cu(ppmma)$Cl_2$]$_2$ and Cu(ppmma)$Br_2$ follow the Curie-Weiss law. No significant intermolecular magnetic interactions were examined in both complexes, and magnetic exchange interactions are discussed on the basis of the structural features.

• Journal of Photoscience
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• v.11 no.32
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• pp.65-69
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• 2004

The mechanism of interaction of four coumarin derivatives (CDS) with bovine serum albumin (BSA) was studied using spectrofluorometric technique. It was found that the coumarin ring common to all CDS makes major contribution to interaction. Binding affinities could be related to parachor values of CDS. Stem-Volmer plots indicated the presence of static component in the quenching mechanism. Results also showed that both tryptophan residues of protein are accessible to CDS. The high magnitude of rate constant of quenching indicated that the process of energy transfer occurs by intermolecular interaction forces and thus CDS binding site is in close proximity to tryptophan residues of BSA. Binding studies in the presence of the hydrophobic probe, 8-anilino-l-naphthalein-sulfonic acid showed that there is hydrophobic interaction between CDS and the probe and they do not share common sites in BSA. Thermodynamic parameters obtained from data at different temperatures showed that the binding of CDS to BSA involve hydrophobic bonds predominantly. The effects of various metal ions on the binding of CDS with BSA were also investigated.

• Proceedings of the Korean Vacuum Society Conference
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• 2012.08a
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• pp.230-230
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• 2012

Graphene have showed promising performance as electrodes of organic devices such as organic transistors, light-emitting diodes, and photovoltaic solar cells. In particular, among various organic materials of graphene-based organic devices, pentacene has been regarded as one of the promising organic material because of its high mobility, chemical stability. In the bottom-contact device configuration generally used as graphene based pentacene devices, the morphology of the organic semiconductors at the interface between a channel and electrode is crucial to efficient charge transport from the electrode to the channel. For the high quality morphology, understanding of initial stages of pentacene growth is essential. In this study, we investigate self-assembly of pentacene molecules on graphene formed on a 6H-SiC (0001) substrate by scanning tunneling microscopy. At sub-monolayer coverage, adsorption of pentacene molecules on epitaxial graphene is affected by $6{\times}6$ pattern originates from the underlying buffer layer. And the orientation of pentacene in the ordered structure is aligned with the zigzag direction of the edge structure of single layer graphene. As coverage increased, intermolecular interactions become stronger than molecule-substrate interaction. As a result, herringbone structures the consequence of higher intermolecular interaction are observed.

• Journal of Photoscience
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• v.12 no.1
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• pp.25-32
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• 2005

Binding of N-Alkyl phenothiazines (NAP) to bovine serum albumin (BSA) was studied by spectroscopic methods.It was found that the phenothiazine ring common to all drugs makes major contribution to interaction. However, the nature of alkylamino group at position 10 influences the protein binding significantly. Stern-Volmer plots indicated the presence of static component in the quenching mechanism. The high magnitude of rate constant of quenching indicated that the process of energy transfer occurs by intermolecular interaction and thus the drug-binding site is in close proximity to tryptophan residues of BSA. Binding studies in presence of hydrophobic probe, 8-anilino-1-naphthalein-sulphonic acid showed that there is hydrophobic interaction between drug and the probe and they do not share common sites in BSA. Thermodynamic parameters obtained from data at different temperatures showed that the binding of NAP to BSA predominantly involve hydrophobic forces. The effects of some cations and anions common ions were investigated on NAP-BSA interactions. The CD spectrum of BSA in presence of drug showedthat binding of drug leads to change in the helicity of the protein.

• Journal of Microbiology and Biotechnology
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• v.23 no.8
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• pp.1107-1115
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• 2013

The Cyt1Aa protein of Bacillus thuringiensis susbp. israelensis elaborates demonstrable toxicity to mosquito larvae, but more importantly, it enhances the larvicidal activity of this species Cry proteins (Cry11Aa, Cry4Aa, and Cry4Ba) and delays the phenotypic expression of resistance to these that has evolved in Culex quinquefasciatus. It is also known that Cyt1Aa, which is highly lipophilic, synergizes Cry11Aa by functioning as a surrogate membrane-bound receptor for the latter protein. Little is known, however, about whether Cyt1Aa can interact similarly with other Cry proteins not primarily mosquitocidal; for example, Cry2Aa, which is active against lepidopteran larvae, but essentially inactive or has very low toxicity to mosquito larvae. Here we demonstrate by ligand binding and enzyme-linked immunosorbent assays that Cyt1Aa and Cry2Aa form intermolecular complexes in vitro, and in addition show that Cyt1Aa facilitates binding of Cry2Aa throughout the midgut of C. quinquefasciatus larvae. As Cry2Aa and Cry11Aa share structural similarity in domain II, the interaction between Cyt1Aa and Cry2Aa could be a result of a similar mechanism previously proposed for Cry11Aa and Cyt1Aa. Finally, despite the observed interaction between Cry2Aa and Cyt1Aa, only a 2-fold enhancement in toxicity resulted against C. quinquefasciatus. Regardless, our results suggest that Cry2Aa could be a useful component of mosquitocidal endotoxin complements being developed for recombinant strains of B. thuringiensis subsp. israelensis and B. sphaericus aimed at improving the efficacy of commercial products and avoiding resistance.