• 한국세라믹학회지
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• 제52권6호
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• pp.483-488
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• 2015

Blast furnace slag(BFS) is well known for its hardening mechanism in ordinary Portland cement with alkali activation due to its latent hydraulic property. The possibility of using calcium compound as activator for BFS has been investigated in this study. The hydration properties of calcium compound activated BFS binders were explored using heat of hydration, powder X-ray diffraction and compressive strength testing. Heat of hydration results indicate that the hydration heat of BFS is lower than OPC paste by about 50%. And ettringite as hydration product was formed continuously as the calcium sulfate was decreased. The maximum compressive strength of hardened BFS mortar at 28 days is confirmed to be 83% as compared with hardened OPC mortar.

• 대한화학회지
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• 제23권6호
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• pp.374-384
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• 1979

Zeolite NaA의 ${\alpha}$ cage에 있어서의 수화에너지와 그 위치를 결정하였다. Na(1)과 Na(2)사이의 site selectivity를 에너지 계산으로부터 결정하였는데 Na(1)이 Na(2)보다 선택성이 있는 것을 알 수 있었다. ${\alpha}$-Cage에 수화된 물들은 일그러진 정 12면체를 형성함을 알 수 있었다. Water(1), Water(2), Water(3)의 평균수화에너지는 각각 -29.847, -25.344, -15.888kcal/mole이다. 이 에너지 계산으로부터 얻어진 수화된 물들의 산소원자의 위치는 X선값과 잘 일치함을 보여준다. 또 수화된 정도에 따른 수화에너지의 그래프를 얻었다. 이 결과는 실험으로부터 얻어진 differential heat of sorption curve와 잘 일치함을 보여준다. ${\alpha}$ Cage 속에서의 유전상수는 3.5가 적합함을 알 수 있었다.

• Bulletin of the Korean Chemical Society
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• 제12권2호
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• pp.143-148
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• 1991

In the unhydrated and hydrated states, conformational free energies of L-ascorbic acid anion (AAA) were computed with an empirical potential function and the hydration shell model (a program CONBIO). The conformational energy was minimized from possible starting conformations expressed with five torsion angles of the molecule. The conformational entropy of each low energy conformation in both states was computed using a harmonic approximation. As found in L-ascorbic acid (AA), intramolecular hydrogen bonds (HBs) are proved to be of significant importance in stabilizing the overall conformations of AAA in both states, and give the folded conformations, which are quite different from those in crystal. There are competitions between HBs and hydration around O3 atom of the lactone ring and hydroxyls of the acyclic side chain. Especially, the whole conformation of AAA is strongly dependent on the water-accessibility of O3 atom. Though there is a significant effect of the hydration on conformational surface, the lowest energy conformation of the unhydrated AAA is conserved. The different patterns of HBs and hydration result in the conformations of AAA in both states being different from those of AA. It can be drawn by several feasible conformations obtained in the hydrated state that there exists an ensemble of several conformations in aqueous solution.

• Bulletin of the Korean Chemical Society
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• 제5권1호
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• pp.27-32
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• 1984

To investigate the hydration effects on the conformational changes of N-pivaloly-L-prolyl-N-methyl-N'-isopropyl-L-alanin amide (PPMIA), the conformational free energy changes have been calculated by using an empirical potential function varying all the independent degrees of freedom of PPMIA backbones. It is found that cis conformers are folded by a strong intramolecular hydrogen bond involving both terminal CO and NH groups whereas trans conformers accommodate the open conformation. Conformers in the free state are proved to be less stable than in the hydrated state. The free energy changes of cis and trans PPMIA due to the hydration are -50.5 and -39.8 kcal/mole, their conformational energy changes are -52.3 and -41.0 kcal/mole, and their conformational entropy changes are -5.9 and -4.0 e.u., respectively. The free energy changes of cis PPMIA to trans PPMIA in the free and hydrated states are 5.3 and 16.0 kcal/mole, their conformational energy changes are 7.6 and 18.8 kcal/mole, and the entropy changes due to the conformational transitions correspond to 7.5 and 9.4 e.u., respectively. From these results, it is found that the bound water molecules play an important role in stabilizing the conformation of PPMIA.

• Bulletin of the Korean Chemical Society
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• 제2권1호
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• pp.24-28
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• 1981

Theoretical studies of the sodium cation binding and the isotope hydration effects on the static model compound B-DNA have been qualitatively elucidated by using empirical potential energy functions. In the first place, the sodium cations bound to phosphate anions and their hydration scheme have been optimized and have given a reasonable agreement with other theoretical results and experimental studies. In the second stage, the isotope effect on the hydration through the substitution of $D_2O\;for\;H_2O$ has been carried out by the same procedure. The stabilization of B-DNA has been explained and compared in terms of the sodium cation binding to phosphate anions and its hydration in both cases of $H_2O\;and\;D_2O$.

• 한국수소및신에너지학회논문집
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• 제33권3호
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• pp.219-225
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• 2022

In this study, as one part of the studies on the mechanical properties of the polymer electrolyte membrane, a study was conducted on the change in the mechanical properties due to hydration before and after aging of the polymer electrolyte membrane. The mechanical properties of the polymer electrolyte membrane changes due to hydration were confirmed through tensile tests of hydrated and non-hydrated Nafion 117. As results of this study, non-hydrated membrane showed higher mechanical properties than hydrated thing in the elastic region and some plastic regions. But, it was confirmed that hydrated membrane exhibited higher mechanical properties than non-hydrated thing in the large plastic region. Hydrated membrane has a lower glass transition temperature than non-hydrated thing due to the role of water as a plasticizer. In addition, the number of ion aggregates decreases, but the size increases, and the hydrated Nafion 117 is thought to have different mechanical properties from that of the non-hydrated thing due to the characteristic that the internal attraction is strengthened.

• 콘크리트학회지
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• 제9권2호
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• pp.121-132
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• 1997

콘크리트의 열해석은 콘크리트 초기온도, 환경조건 및 시멘트의 수화 등에 의해 특징지워진다. 이러한 상호관계를 모두 고려한 프로그램을 만들어서, 콘크리트재료의 열특성과 환경조건을 감안한 콘크리트 구조물의 온도해석을 하였다. 시멘트 수화의 특성으로는 활성화에너지, 단위열량, 수화열이 있으며 이러한 인자들에 의해 콘크리트의 내부열 발생이 영향을 받는다. 본 연구에서는 활성화에너지와 수화열을 상대강도-등가재령모델에 의해 구했으며, 단위열량은 등온열량측정법에 의해 실험적으로 구하였다. 또한 콘크리트 구조물의 온도분포를 실험적으로 구하여 수치해석모델과 비교하였다. 먼저 위에서 제시된 모든 조건들에 대한 parametric 해석을 실시하여 프로그램의 신뢰성을 확보하였다. 그리고 원주형시편을 만들어서 온도분포 및 변화를 측정하여 수치해석에 의해 예측된 온도분포와 비교하였다.

• 약학회지
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• 제40권6호
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• pp.632-639
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• 1996

Most stable conformers of some antiinflammatory fenamates were obtained by conformational free energy change calculations. Conformational energies for the molecules as unhydrate d state were estimated first, and those as hydrated state were calculated then to simulate the molecules in aqueous solution using a hydration shell model. The initial geometries of the molecules were obtained either from X-ray crystallographic data or from homologous molecular fragments. The bond lengths and angles were not varied, but all the torsion angles were varied step by step during the conformational free energy surface searching. The results show that there are several feasible conformations for a compound. And the molecules are somewhat stabilized by hydration (-${\delta}G_{hyd}{\cong}$13 to 16kcal/mole), but the conformations were not changed significantly by the hydration itself. There seems to be a strong tendency of intramolecular hydrogen bonding between imino hydrogen and carboxyl oxygen of the compounds. As a result, the carboxyl group cannot be rotated freely, and the rotation of the second aromatic ring is the main reason for the conformational variations of the compounds. The ECEPP force fields via the program CONBIO were used throughout this study.

• Computers and Concrete
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• 제19권6호
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• pp.659-666
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• 2017

Based on the Arrhenius equations, several hydration exothermic models that precisely calculate the influence of concrete's self-temperature duration on its hydration exothermic rate have been presented. However, the models' convergence is difficult to achieve when applied to engineering projects, especially when the activation energy of the Arrhenius equation is precisely considered. Thus, the models' convergence performance should be improved. To solve this problem and apply the model to engineering projects, the relationship between fast iteration and proper expression forms of the adiabatic temperature rise, the coupling relationship between the pipe-cooling and hydration exothermic models, and the influence of concrete's self-temperature duration on its mechanical properties were studied. Based on these results, the rapid convergence of the hydration exothermic model and its coupling with pipe-cooling models were achieved. The calculation results for a particular engineering project show that the improved concrete hydration exothermic model and the corresponding mechanical model can be suitably applied to engineering projects.

• EDISON SW 활용 경진대회 논문집
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• 제5회(2016년)
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• pp.163-166
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• 2016

Hydrophobicity is the key concept to understand the water plays in protein folding, protein aggregation, and protein-protein interaction. Traditionally, the hydrophobicity of protein is defined based on the scales of the hydrophobicity of residue, assuming that the hydrophobicity of free amino acids is maintained. Here, we explore how the hydrophobicity of constituting amino acids in protein rely on the protein context, in particular, on the total charge and secondary structures of a protein. To this end, we calculate and investigate the hydration free energy of three short proteins based on the integral-equation theory of liquids. We find that the hydration free energy of charged amino acids is significantly affected by the protein total charge and exhibits contrasting behavior depending on the protein total charge being positive or negative. We also observe that amino acids in the ${\beta}-sheets$ display more enhanced the hydrophobicity than amino acids in the loop, whereas those in the ${\alpha}-helix$ do not clearly show such a tendency. And the salt-bridge forming amino acids also exhibit increase of the hydrophobicity than that with no salt bridge. Our results provide novel insights into the hydrophobicity of amino acids, and will be valuable for rationalizing and predicting the strength of water-mediated interaction involved in the biological activity of proteins.