• Bulletin of the Korean Chemical Society
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• 제15권9호
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• pp.748-751
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• 1994

Poly(ethylene oxide) (PEO) in aqueous solutions has a hydrophobic character which can induce the hydrophobic interaction between its nonpolar parts. The hydrophobic properties of aqueous PEO solutions are studied by the viscometry in terms of the water structure-making and -breaking capabilities of added solutes of ureas. The results show that the contracted conformation of PEO of low molecular weight, namely poly(ethylene glycol) (PEG), does not result from the hydrophobic interaction between the nonpolar parts of PEO but it can participate in a hydrophobic interaction between the nonpolar parts of PEO and added ureas solutes with nonpolar groups, which can induce a large hydrodynamic volume and increase the viscosity. On the other hand, the PEO of large molecular weight seems to behave like any other water soluble polymers with nonpolar parts and its conformation in aqueous solutions is well explained in terms of water structure perturbing capabilities of added ureas.

• International Journal of Industrial Entomology and Biomaterials
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• 제33권2호
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• pp.144-148
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• 2016

Recently, silk sericin has been studied extensively for biomedical and cosmetic applications because of its unique properties, including UV resistance and wound healing ability. For use in applications, sericin is fabricated in various forms including films and gels. However, the mechanical properties of sericin are too weak. In this basic study on improving the mechanical properties of sericin, a silk sericin aqueous solution was separated into two layers by centrifugation. The solution viscosity, molecular conformation, and mechanical properties of each separation layer of the sericin were examined. Sericin from the lower layer had a higher solution viscosity and film mechanical properties (strength and strain) than that from the upper layer, implying that sericin from the lower layer had a higher molecular weight than that from the upper layer. The molecular conformation of the sericin films varied depending on the casting solvent. In aqueous solution, the sericin film from the lower layer showed a ${\beta}$-sheet conformation, whereas that from the upper layer displayed a random coil conformation. All the sericin films showed a highly ${\beta}$-sheet-crystallized state when cast in formic acid, regardless of the separation layer.

• Archives of Pharmacal Research
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• 제13권1호
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• pp.43-50
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• 1990

Conformational free energy calculations using an empirical potential function (ECEPP/2) and hydration shell model were carried out on the four-4-aminodiphenyl sulfone analogues of 4, 4'-diamino-2' methyldiphenyl sulfone, 4, 2', 4-triaminodiphenyl sulfone, 4, 4'-diaminodiphenyl sulfone, and 4-aminodiphenyl sulfone as antibacterial agents on Mycobacterium lufu. The conformational energy was minimized from starting conformations which included possible combinations of torsion angles in the molecule. The conformational entropy change of each conformation was computed using a harmonic approximation. To understand the hydration effect on the conformation of the molecule in aqueous solution, the contributions of water-accessible volume and the hydration free energy of each group or atom in the lowest-free-energy conformation was calculated and compared each other. From comparison of the computed lowest-free-energy conformations of four analogues with their antibacterial activities, it is known that the conformation and the hydrophobicity of sulfonyl group and its adjacent carbon atom in each compound are the essential factors to show the strong antibacterial activity.

• 약학회지
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• 제33권6호
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• pp.350-360
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• 1989

The conformation and activity of the four benzenesulfonyl analogues of 4-aminobenzene-sulfonamide, 4-aminobenzenesulfonic acid, 4-methylbenzenesulfonamide, and 4-methylbenzenesulfonic acid with antibacterial activity on Staphylococcus aureus were studied using an empirical potential function (ECEPP/2) and the hydration shell model. The conformational energies were minimized from the starting conformations which included possible combinations of torsion angles in each molecule. To understand the hydration effect on the conformation of the molecule in aqueous solution, the hydration free energy of each group was calculated and compared each other. The conformational entropies of low-free-energy coformation of benzenesulfonly analogues were computed by a harmonic approximation. From the correlation of lowest-free-energy conformation of each compound and its antibacterial activity, it was found that the hydration of sulfonyl groups and the substituents are the decisive factors to show antibacterial activities.

• 한국생물물리학회:학술대회논문집
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• 한국생물물리학회 1996년도 정기총회 및 학술발표회
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• pp.28-28
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• 1996

NMR studies on the structure of the luteinizing hormone releasing hormone (LHRH) in aqueous buffer and trifluoroethanol (TFE)/aqueous buffer (1:1, v/v) solution were performed. The NMR data under these conditions suggested a unique conformation which includes a ${\beta}$-1 turn of the Tyr5-Arg8 segment and an unusual turn of Ser4-Gly6 segment staggered with the ${\beta}$-I turn. (omitted)

• Bulletin of the Korean Chemical Society
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• 제11권2호
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• pp.144-149
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• 1990

Conformational free energy calculations using an empirical potential function (ECEPP/2) and the hydration shell model were carried out on the sulfonylurea herbicides of bensulfuron methyl (Londax) and metsulfuron methyl (Ally). The conformational energy was minimized from starting conformations which included possible combinations of torsion angles in the molecule. The conformational entropy of each conformation was computed using a harmonic approximation. To understand the hydration effect on the conformation of the molecule in aqueous solution, the hydration free energy of each group was calculated and compared each other. It was found that the low-free-energy conformations of two molecules in aqueous solution prefer the overall folded structure, in which an interaction between the carbonyl group of ester in aryl ring and the first amido group of urea bridge plays an important role. From the analysis of total free energy, the hydration and conformational entropy are known to be essential in stabilizing low-free-energy conformations of Londax, whereas the conformational energy is proved to be a major contribution to the total free energy of low-free-energy conformations of Ally.

• Bulletin of the Korean Chemical Society
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• 제25권6호
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• pp.838-842
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• 2004

Amyloid peptide (A${\beta}$) is the major component of senile plaques found in the brain of patient of Alzheimer's disease. ${\beta}$-amyloid peptide (25-35) (A${\beta}$25-35) is biologically active fragment of A${\beta}$. The three-dimensional structure of A${\beta}$25-35 in aqueous solution with 50% (vol/vol) TFE determined by NMR spectroscopy previously adopts an ${\alpha}$-helical conformation from $Ala^{30}$ to $Met^{35}$. It has been proposed that A${\beta}$(25-35) exhibits pH- and concentration-dependent ${\alpha}-helix{\leftrightarrow}{\beta}$sheet transition. This conformational transition with concomitant peptide aggregation is a possible mechanism of plaque formation. Here, in order to gain more insight into the mechanism of ${\alpha}$-helix formation of A${\beta}$25-35 peptide by TFE, which particularly stabilizes ${\alpha}$-helical conformation, we studied the secondary-structural elements of A${\beta}$25-35 peptide by molecular dynamics simulations. Secondary structural elements determined from NMR spectroscopy in aqueous TFE solution are preserved during the MD simulation. TFE/water mixed solvent has reduced capacity for forming hydrogen bond to the peptide compared to pure water solvent. TFE allows A${\beta}$25-35 to form bifurcated hydrogen bonds to TFE as well as to residues in peptide itself. MD simulation in this study supports the notion that TFE can act as an ${\alpha}$-helical structure forming solvent.

• 한국잠사곤충학회지
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• 제37권2호
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• pp.142-153
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• 1995

특이한 분자 구조를 가진 생체 고분자로서 유용한 견 피브로인은 다양하게 성형 가공할 수 있으며 이를 위해서는 견 피브로인 수용액을 필요로 한다. 견 피브로인의 용해 조건이 형성되는 견 피브로인의 분말과 필름에 미치는 영향을 알아보기 위하여 종성염과 산가수분해법으로 견 피브로인을 용해시킨 수용액으로부터 견 피브로인 분말과 필름을 제조하고 이들의 특성을 아미노산 조정 분석, SEM, DSC, IR, X-ray Diffraction 등의 방법을 통하여 조사 분석한 결과는 다음과 같다. 1. 염화칼슘법과 염산법에 의해 피브로이을 용해시켰을 때 처리에 따라 아미노산 조성은 달랐으며 분자량도 차이가 있었다. 2. 분말의 구조 분석 결과, 염화칼슘법에 의한 처리에서 열분해 온도는 대조에 비해 낮게 나타났고 무정형의 분자 구조를 띄고 있음을 알 수 있었다. 염산 처리에 의한 잔유물은 대조보다 높은 온도에서 $\beta$구조에 의한 분해 거동을 보였으며 높은 결정화도를 나타냈다. 한편 염산에 용해된 부분은 열분해 분석 결과 a-helix에 의한 흡열 peak을 나타냈다. 3. 염화칼슘법에 의해 형성된 견 피브로인 필름은 모정형에 가까운 결정 구조를 가지고 있지만 불용화 처리에 의해 결정성이 향상됨에 따라 피브로인 필름의 흡습율은 감소하였으며, 열분해 온도가 증가했다.

• 한국자기공명학회논문지
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• 제2권1호
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• pp.41-49
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• 1998

A linear undecapeptide, Substance P (SP) is involved in a wide variety of physiological processes such as pain, inflammation, salivation, and hypertension. Tertiary structure of SP in dodecylphosphocholine (DPC) micelles has been investigated by CD, NMR spectroscopy, and DGII calculation. CD spectrum of SP in the presence of 7.5 mM DPC micelles does not show any favorable secondary structure. The tertiary structure determined by NMR spectroscopy and DGII calculation shows that the Phe7-Phr8-Gly9-Leu10 region adopts a turn structure, while the N-terminal region is quite flexible. Both prolines in SP exist preferentially as the trans isoforms and the aromatic ring of Phe7 protrudes outward. Conformation of SP may be restrained by the contact of the Phe7 aromatic ring with the hydrophobic side chains of the DPC micelles and this interaction induces a turn structure. Structure of SP in aqueous solution in the presence of DPC micelles can represent a good model to study the conformation recognized by the receptor near neutral membrane.

• 약학회지
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• 제36권6호
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• pp.518-528
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• 1992

To determine the optimal conformation of sulfonylureas, the correlation between conformation and hypoglycemic activity of the two sulfonylureas of tolbutamide and chlorpropamide as hypoglycemic agent was studied using an empirical potential function (ECEPP/2) and the hydration shell model in the unhydrated and hydrated states. The conformational energy was minimized from several starting conformations with possible torsion angles in each molecule. The conformational entropy change of each conformation was computed using a harmonic approximation. To understand the hydration effect on the conformation of the molecules in aqueous solution, the contribution of water-accessible volume of each group or atom in the lowest-free-energy conformation was calculated and compared each other. From comparison of the computed lowest-free-energy conformations of two sulfonylureas, it could be suggested that the hydration of sulfonylurea moiety is related to increase the hypoglycemic activity. From the calculation results, it was known that the conformational entropy is the major contribution to stabilize the low-free-energy conformations of two sulfonylureas in unhydrated state. Whereas, in hydrated state, the hydration free energy largely contributes to the total free energies of low-free-energy conformations of tolbutamide and conformational entropy contributes to stabilize the low-free-energy conformations of chlorpropamide. The torsion angles from phenyl ring to urea moiety of the low-free-energy conformations of the two sulfonylureas were shown the nearly regular trend. On the basis of these results, the conformation exhibiting the optimal hypoglycemic activity of sulfonylureas and the binding direction to pancreatic receptor site A could be predicted. Also, according to the side chain lengthening of urea moiety, tolbutamide showed various conformational change. Therefore, steric effect may be important factor in the interaction between sulfonylureas and the putative pancreatic receptor.