• 한국미생물·생명공학회지
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• 제13권3호
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• pp.257-263
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• 1985

Rhodopseudomonas sp. KCTC 1437은 글루타민산이 질소원으로 존재할 때, 포도당으로부터 질소고 정효소 (nitrogenase)에 의해 효율적으로 수소를 생성하였다. in vivo에서 질소고정 효소의 활성도를 조사해 본 결과, 암모니아 이온의 제한 농도에서 키운 균체가 다른 질소원에서 키운 균체보다 더 큰 정도로 수소를 글루타민산 존재하에서 포도당으로부터 생성하였다. 이 균주는 또한 수소 생성의 억제물질 및 조건으로 알려져 있는 암모니아 이온의 높은 농도와 암조건에서 높은 정도로 수소를 생성했는데 이것은 수소효소 (hydrogenase)의 일종인 포르믹산 수소분해효소 (formic hydrogenlyase)에 의한 것이라 고려된다.

• 한국식물학회:학술대회논문집
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• 한국식물학회 2001년도 춘계학술발표대회:발표눈문요지록
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• pp.8-8
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• 2001

• Journal of Microbiology and Biotechnology
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• 제5권3호
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• pp.177-180
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• 1995

In horseradish peroxidase-catalyzing polymerization of phenol under the water/dioxane solvent system, the optimal concentration of hydrogen peroxide was found to be 10 mmol/I. Feeding of hydrogen peroxide at its optimal concentration improved the polymerization performance by reducing reaction time and increasing molecular weights. Monomer conversions and the molecular weights of the enzymatically produced polymer were in the ranges of 83.1~94.2$%$ and 58000~68000, respectively.

• 한국진공학회:학술대회논문집
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• 한국진공학회 2011년도 제41회 하계 정기 학술대회 초록집
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• pp.205-205
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• 2011

The self-assembly of ${\gamma}$-phenylalanine on Au(111) at 150 K was investigated using scanning tunneling microscopy (STM). Phenylalanine can potentially form two-dimensional (2D) molecular networks through hydrogen bonding (through the carboxyl and amino groups) and ${\pi}-{\pi}$ stacking interactions (via aromatic rings). We found that ${\gamma}$-phenylalanine molecules self-assembled on Au(111) surfaces into well-ordered structures such as ring-shaped clusters (at low and intermediate coverages) and 2D molecular domains (intermediate and monolayer coverages), whereas ${\alpha}$-phenylalanine molecules formed less-ordered structure on Au(111). The self-assembly of ${\gamma}$- but not ${\alpha}$-phenylalanine may be related to the flexibility of the carboxyl and amino groups in the molecule. Moreover, as expected, the 2D molecular network of ${\gamma}$-phenylalanine on Au(111) was mediated by a combination of hydrogen bonding and ${\pi}-{\pi}$ stacking interactions.

• Molecules and Cells
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• 제27권6호
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• pp.651-656
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• 2009

The formation of ${\beta}$-amyloid peptide ($A{\beta}$) is initiated from cleavage of amyloid precursor protein (APP) by a family of protease, ${\alpha}$-, ${\beta}$-, and ${\gamma}$-secretase. Sub W, a substrate peptide, consists of 10 amino acids, which are adjacent to the ${\beta}$-cleavage site of wild-type APP, and Sub M is Swedish mutant with double mutations on the left side of the ${\beta}$-cleavage site of APP. Sub W is a normal product of the metabolism of APP in the secretary pathway. Sub M is known to increase the efficiency of ${\beta}$-secretase activity, resulting in a more specific binding model compared to Sub W. Three-dimensional structures of Sub W and Sub M were studied by CD and NMR spectroscopy in water solution. On the basis of these structures, interaction models of ${\beta}$-secretase and substrate peptides were determined by molecular dynamics simulation. Four hydrogen bonds and one water-mediated interaction were formed in the docking models. In particular, the hydrogen bonding network of Sub M-BACE formed spread over the broad region of the active site of ${\beta}$-secretase (P5-P3'), and the side chain of P2- Asn formed a hydrogen bond specifically with the side chain of Arg235. These are more favorable to the cleavage of Sub M by ${\beta}$-secretase than Sub W. The two substrate peptides showed different tendency to bind to ${\beta}$-secretase and this information may useful for drug development to treat and prevent Alzheimer's disease.

• 폴리머
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• 제35권5호
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• pp.444-450
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• 2011

천연 알지네이트를 저분자화시키기 위해 과산화수소/초음파를 사용하였다. 이때 반응 온도 시간, 과산화수소 농도 그리고 초음파 조사 조건 등이 저분자화 생성물에 미치는 영향을 검토하였다. 생성된 저분자 알지네이트의 화학적 구조를 규명한 결과 주로 1,4-glycosidic bond가 끓어져서 저분자화가 진행되고 특정조건에서 생성물에 formate 그룹이 형성됨을 확인할 수 있었다. 생성물의 분자량은 MALS가 부착된 GPC를 사용하여 측정하였다. 2 wt%의 고분자 알지네이트 용액을 50 $^{\circ}C$의 초음파 분위기에서 0.5시간 동안 반응시켰을 때 분자량이 450 kDa에서 15.9 kDa로 저하되었다. 또한 분자량분포도는 상당히 좁고 반응 조건에 따라 큰 변화 없이 일정함(~2)을 확인할 수 있었다.

• 대한화학회지
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• 제32권3호
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• pp.249-259
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• 1988

Methanol, ethanol, acetone, dimethylsulfoxide, N,N-dimethylformamide, tetrahydrofuran, dioxane, 및 acetonitrile의 8가지 분자에 대한 용매효과를 고찰할 목적으로 메탄올을 양성자로 하고, 8가지 분자를 양성자 받게로 하여, 이들 이합체를 AM1 Hamiltonian법과 supermolecule법에 의해 monomer 및 dimer의 optimized geometry, electron density, molecular energy 및 hydrogen-bonding energy를 계산하였다. 그 결과로 각 dimer의 hydrogen-bonding에 기여하는 stabilization energy 순서는 dimethylsulfoxide > ethanol > N,N-dimethylformamide > acetone > methanol > tatrahydrofuran > dioxane > acetonitrile임을 알았으며 이 안정성의 순서를 electron density의 변화 및 energy partition의 결과로 설명하였다.

• Bulletin of the Korean Chemical Society
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• 제30권2호
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• pp.482-485
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• 2009

• Bulletin of the Korean Chemical Society
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• 제31권9호
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• pp.2717-2720
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• 2010

• Journal of Microbiology and Biotechnology
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• 제23권6호
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• pp.750-758
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• 2013

Anthrax is a bacterial disease caused by the aerobic spore-forming bacterium Bacillus anthracis, which is an important pathogen owing to its ability to be used as a terror agent. B. anthracis spores can escape phagocytosis and initiate the germination process even in antimicrobial conditions, such as oxidative stress. To analyze the oxidative stress response in B. anthracis and thereby learn how to prevent antimicrobial resistance, we performed protein expression profiling of B. anthracis strain HY1 treated with 0.3 mM hydrogen peroxide using a comparative proteomics-based approach. The results showed a total of 60 differentially expressed proteins; among them, 17 showed differences in expression over time. We observed time-dependent changes in the production of metabolic and repair/protection signaling proteins. These results will be useful for uncovering the metabolic pathways and protection mechanisms of the oxidative response in B. anthracis.