• Proceeding of EDISON Challenge
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• 2014.03a
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• pp.263-274
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• 2014

펩타이드 중합체의 이차 구조는 화학적, 생물학적 기능을 갖는 단백질 삼차 구조를 결정하는 중요한 구성요소이다. 이러한 단백질의 이차구조에 대한 정보는 치매, 광우병과 같은 단백질 응집관련 질병에서 응집유발 단백질의 형성과정 및 안정도와 밀접한 연관이 있다. 본 연구는 폴리알라닌을 모델 펩타이드로 선택하여, 이들의 가능한 7가지 이차구조들에 대한 구조적, 열역학적 특성을 계산화학방법을 통해 비교 분석하였다. 우선 기체상에서 7가지 구조들의 구조최적화를 통해 상대적 안정도를 비교하였고, 나아가 EDISON의 용매화 자유 에너지의 열역학적 계산방법을 통해 수용액상에서의 상대적인 안정도와 그 원인을 비교, 분석하였다. 특히, 기체상에서와 수용액상애서 폴리알라닌 이차구조들의 상대적 안정도가 바뀌는 원인에 대해, 폴리알라닌의 구조적 특징과 수소결합과의 상관관계를 통해 규명하였다. 본 연구에서 밝힌 단백질 이차 구조의 상대적 안정도 및 물과의 상관관계에 미치는 구조적, 열역학적 원인은 응집 유발 단백질에서 제시된 특정 이차 구조의 선택적 안정성에 대한 근거를 제시하며, 그 기작을 이해하는 중요한 단서를 제공한다.

• Journal of the Korean Society of Radiology
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• v.18 no.3
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• pp.239-248
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• 2024

Radiation therapy uses high energy, which can have side effects on the human body. Therefore, it is important to ensure that the appropriate dose is set for irradiation and to have confidence in the radiation produced by the generator. The EPR/Alanine dosimetry system is characterized by water equivalence, dose response linearity, and low fading, which makes it useful for quality control of radiation therapy equipment. In this study, we compared the signal and dose response curves of EPR/Alanine dosimetry by mass of alanine using 6 MV energy of a LINAC. An alanine dosimeter and EPR spectrometer from Burker, and a LINAC from Elekta, were used. A dose response curve and a 1st order regression equation were constructed from the irradiated dose and the EPR signal from the alanine dosimeter. We compared the signal magnitude and dose response curve with mass and checked the confidence through the measurement uncertainty of the dose response curve. As a result, it was found that the magnitude of the EPR signal increased by about 1.3 times at 64.5 mg, and the sensitivity of the dose response curve increased as the mass increased. The measurement uncertainty was evaluated to be between 5.84 % and 8.93 %. Through this study, it is expected that the EPR/alanine dosimetry system can be applied to the quality assurance and quality control of a LINAC.

• Journal of the Korean Chemical Society
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• v.54 no.6
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• pp.680-686
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• 2010

Inhibition effects of alanine(Ala), asparagine(Asn), aspartic acid(Asp), glutamine(Gln) and methionine(Met) on the corrosion of copper were investigated in aerated artificial sea water. Amino acid adsorption process in copper surface can be explained by Temkin logarithmic isotherm due to the interaction between the adsorbed molecules. The inhibition efficiency for the copper corrosion depended on the concentration of amino acids.

• Proceedings of the KSCN Conference
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• 1998.11a
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• pp.117-117
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• 1998

• Proceedings of the KSCN Conference
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• 1998.11a
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• pp.118-118
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• 1998

• Journal of Life Science
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• v.9 no.2
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• pp.146-152
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• 1999

In order to elucidate a role of residue 24 in the folding of tryptophan synthase $\alpha$ subunit, mutant proteins in which Thr 24 was replaced by Met, Ala, Ser, Leu or Lys were overexpressed in E. coli, and the extents of accumulated proteins as soluble or aggregated forms were examined. The mutant proteins with Met or Leu at residue 24 were predominantly accumulated as soluble forms as the native protein. On the other hand, mutant proteins with Ser, Ala or Lys at residue 24 were expressed as aggregated forms as well. This result suggests that residue 24 of tryptophan synthase $\alpha$ subunit may be implicated in the folding of this protein.

• Journal of the Korean Chemical Society
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• v.29 no.1
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• pp.31-37
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• 1985

N-Acetyl-1-phenylalanyl-1-phenylalanine methyl ester (APhPhMe), N-acetyl-l-phenylalanine methyl ester (APhMe) and N-acetyl-1-phenylalanyl-1-alanine methyl ester (APhAlMe) were used as model compounds to investigate a protein denaturation under various temperatures and pressures. Overall, the solubility of APhPhMe in water increased with increasing pressure and that of APhMe decreased. However, the solubility of APhAlMe was nearly same. The values of volume change of APhPhMe were -0.9, -1.47, -1.09, -1.52 ml/mole at 20, 30, 40 and 50$^{\circ}C$, respectively, and those of APhMe were +6.0, +7.0, +7.5 ml/mole at 20, 30 and 40$^{\circ}C$, respectively. But those of APhAlMe were nearly zero at the measured temperature. The experimental result seems to be explained by the hydrophobic interaction and hydrogen bond of peptide bonds. In the compounds which have only peptide bonds and which have both a pretty large hydrophobic group and a peptide bond in the molecules, the hydrogen bond between peptide bonds is more dominant than the hydrophobic interaction. However, when the number of peptide bond and hydrophobic group increase simultaneously, the hydrophobic interaction seems to be more dominant.

• Proceedings of the Korean Society of Applied Pharmacology
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• 1993.04a
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• pp.157-157
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• 1993

TMI는 알라닌과 글리신이 풍부한 18개의 아미노산으로 이루어져 분자량이 약 1,400Da인 물질이었으며, 가수분해 효소 처리후 억제력의 변화를 보이지 않았고, Porcine liver, spleen, testis에서 정제한 PM II에 대하여 TMI가 비상경적 억제작용을 하는 것으로 나타났으며, Ki value는 각각 300 nM, 250 nM 297 nM이었다. 그리고 돼지 간장에서 부분정제한 PM I, PM II, PM III, phospholipid methytransferase에 대한 정제된 TMI의 영향을 조사해 보면 각각 33%, 47%, 31%, 35%의 억제효과를 나타내었다.

• Proceedings of the Korean Society of Fisheries Technology Conference
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• 2001.10a
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• pp.161-162
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• 2001

복어는 저칼로리, 고단백질 식품으로 각종 무기질 및 비타민이 함유되어 있으며 알콜의 해독작용이 있는 사실이 증명되어 관심을 모으고 있다. 또한 복국은 시원하고 대단히 담백하여 일반인들에게 인기가 있어서 복국집이 많이 늘어나고 있다. 복국의 맛의 주체는 감칠맛 성분인 이노신산(IMP), 그리고 단맛을 내는 글리신과 알라닌등의 작용에 의한 것이다. (중략)

• Journal of the Korean Chemical Society
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• v.63 no.6
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• pp.427-434
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• 2019

The role of hydrophobic residues on protein folding reaction was studied by folding kinetics measurements in conjunction with protein engineering. The HubWA, which was derived from human ubiquitin by mutating the residues at 45 (Phe to Trp) and 26 (Val to Ala), was used as a mutational background. Fourteen hydrophobic residues were mutated to alanine. Among fourteen variants generated, only four variant proteins (V5A, I13A, V17A, and I36A) were suitable for folding study. The folding kinetics of these variants was measured by stopped-flow fluorescence spectroscopy. The folding kinetics of HubWA and V17A was observed to follow a three-state on-pathway mechanism. On the other hand, folding kinetics of V5A, I13A, and I36A was observed to follow a two-state mechanism. Based on these observations, transition of protein folding reaction from collision-diffusion mechanism to nucleation-condensation mechanism was discussed.