• 한국환경보건학회지
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• 제30권4호
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• pp.308-313
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• 2004

Native and acetylated soybean protein with acetylation percentage of $25\%$ were incubated with glucose to induce Maillard reaction. Acetylation of ${\varepsilon}$-amino group of lysine residues changed the conformation of soybean protein. The direct uv spectrum of native and acetylated soybean protein showed conformational changes with accessibility of tyrosine and tryptophan residues increased. Acetylation suppressed Maillard reaction between soybean protein and glucose. Acetylated soybean protein showed improved water sorption, fat binding, foam formation, and emulsion activity of the protein, but depressed brown pigment development and trypsin digestion. Thus aceylation prevented deterioration of certain functional characteristics that occurred during storage, besides causing functional characteristics to be improved on its own.

• 한국자기공명학회논문지
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• 제23권3호
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• pp.67-72
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• 2019

Caveolae are small plasma membrane invaginations that play many roles in signal transduction, endocytosis, mechanoprotection, lipid metabolism. The most important protein in caveolae is the integral membrane protein, caveolin, which is divided into three families such as caveolin 1, caveolin 2, and caveolin 3. Caveolin 1 and 3 are known to incorporate palmitate through linkage to three cysteine residues. Regulation of the protein palmitoylation cycle is important for the cellular processes such as intracellular localization of the target protein, membrane association, conformation, protein-protein interaction, and activity. However, the detailed aspect of individual palmitoylation has not been studied. In the present work, the role of each lipid modification at three cysteines was studied by NMR. Our results suggest that each lipid modification at the natively palmitoylation site has its own roles. For example, lipidations to C106 and C129 are play a role in structural stabilization, however, interestingly, lipid modification to C116 interrupts the structural stabilization.

• 한국생물물리학회:학술대회논문집
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• 한국생물물리학회 1997년도 학술발표회
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• pp.38-38
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• 1997

Serpins (serine protease inhibitor) are single polypeptide proteins of around 400 amino acids, and have a conserved secondary structure consisted of three ${\beta}$-sheets and nine ${\alpha}$-helices. Native conformation of inhibitory serpins is a metastable and requires conformational changes to inhibit target protease.(omitted)

• Bulletin of the Korean Chemical Society
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• 제29권12호
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• pp.2403-2406
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• 2008

• Bulletin of the Korean Chemical Society
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• 제35권8호
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• pp.2494-2504
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• 2014

P38 mitogen activated protein (MAP) kinase is an important anti-inflammatory drug target, which can be activated by responding to various stimuli such as stress and immune response. Based on the conformation of the conserved DFG loop (in or out), binding inhibitors are termed as type-I and II. Type-I inhibitors are ATP competitive, whereas type-II inhibitors bind in DFG-out conformation of allosteric pocket. It remains unclear that how these allosteric inhibitors stabilize the DFG-out conformation and interact. Organosilicon compounds provide unusual opportunity to enhance potency and diversity of drug molecules due to their low toxicity. However, very few examples have been reported to utilize this property. In this regard, we performed docking of an inhibitor (BIRB) and its silicon analog (Si-BIRB) in an allosteric binding pocket of p38. Further, molecular dynamics (MD) simulations were performed to study the dynamic behavior of the simulated complexes. The difference in the biological activity and mechanism of action of the simulated inhibitors could be explained based on the molecular mechanics/generalized Born surface area (MM/GBSA) binding free energy per residue decomposition. MM/GBSA showed that biological activities were related with calculated binding free energy of inhibitors. Analyses of the per-residue decomposed energy indicated that van der Waals and non-polar interactions were predominant in the ligand-protein interactions. Further, crucial residues identified for hydrogen bond, salt bridge and hydrophobic interactions were Tyr35, Lys53, Glu71, Leu74, Leu75, Ile84, Met109, Leu167, Asp168 and Phe169. Our results indicate that stronger hydrophobic interaction of Si-BIRB with the binding site residues could be responsible for its greater binding affinity compared with BIRB.

• 한국식품과학회지
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• 제25권3호
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• pp.277-281
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• 1993

콜로이드 식품에서의 단백질의 구조적 안정성을 연구하기 위하여 7개의 BSA structural intermediates, succinylated ${\beta}-lactoglobulin$을 만든 후 CD, 이황화물 결합함량, hydrodynamic radius 등을 측정하여 그 구조적 특성을 규명했다. Refolding time이 길수록 BSA intermediates들은 native BSA 구조에 근접하는 것을 나타냈고 succinylation은 ${\beta}-lactoglobulin$의 순 음전하를 변화시켜 보다 aperiodic structure를 갖게하였다. Perchlorate 존재하 ${\beta}-casein$의 구조는 소수성 상호작용에 크게 영향 받는 것으로 나타났다.

• Bulletin of the Korean Chemical Society
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• 제30권11호
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• pp.2723-2728
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• 2009

The conformational properties of oligosaccharides are important to understand carbohydrate-protein interactions. A trimannoside, methyl 3,6-di-O-($\alpha$-D-Man)-$\alpha$-D-Man (TRIMAN) is a basic unit of N-linked oligosaccharides. This TRIMAN moiety was further modified by GlcNAc (BISECT), which is important to biological activity of N-glycan. To characterize the trimannoside and its bisecting one we performed a molecular dynamics simulation in water. The resulting models show the conformational transition with two major and minor conformations. The major conformational transition results from the $\omega$ angle transition; another minor transition is due to the $\psi$ angle transition of $\alpha$ (1 $\rightarrow$ 6) linkage. The introduction of bisecting GlcNAc on TRIMAN made the different population of the major and minor conformations of the TRIMAN moiety. Omega ($\omega$) angle distribution is largely changed and the population of gt conformation is increased in BISECT oligosaccharide. The inter-residue hydrogen bonds and water bridges via bisecting GlcNAc residue make alterations on the local and overall conformation of TRIMAN moiety. These changes of conformational distribution for TRIMAN moiety can affect the overall conformation of N-glycan and the biological activity of glycoprotein.

• Bulletin of the Korean Chemical Society
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• 제20권3호
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• pp.301-306
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• 1999

Hepatitis C virus (HCV) has been known to be an enveloped virus with a positive strand RNA genome and the major agent of the vast majority of transfusion associated cases of hepatitis. For viral replication, HCV structural proteins are first processed by host cell signal peptidases and NS2/NS3 site of the nonstructural protein is cleaved by a zinc-dependent protease NS2 with N-terminal NS3. The four remaining junctions are cleaved by a separate NS3 protease. The solution conformations of NS4B/5A, NS5A/5B substrates and NS5A/5B inhibitor have been determined by two-dimensional nuclear magnetic resonance (NMR) spectroscopy. NMR data suggested that the both NS5A/5B substrate and inhibitor appeared to have a folded tum-like conformation not only between P1 and P6 position but also C-terminal region, whereas the NS4B/5A substrate exhibited mostly extended conformation. In addition, we have found that the conformation of the NS5A/5B inhibitor slightly differs from that of NS5A/5B substrate peptide, suggesting different binding mode for NS3 protease. These findings will be of importance for designing efficient inhibitor to suppress HCV processing.

• 대한약학회:학술대회논문집
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• 대한약학회 2002년도 Proceedings of the Convention of the Pharmaceutical Society of Korea Vol.2
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• pp.330.2-330.2
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• 2002

The conformational study on cyclic Ac-Cys-Pro-Xaa-Cys-NHMe (Ac-CPXC-NHMe: X = Ala, Val. Leu. Aib. Gly. His. Phe, Tyr. Asn. and Ser) peptides has been carried out using the ECEPP/3 force field and the hydration shell model in the unhydrated and hydrated states. This work has been undertaken to investigate structural implications of the CPXC sequence as the chain reversal for the initiation of protein folding and as the motif for active site of disulfide oxidoreductases. The backbone conformation DAAA is in common the most feasible for cyclic CPXC peptides in the hydrated state. which has a type 1${\beta}$-turn at the Pro-Xaa sequence. The proline residue and the hydrogen bond between backbones of two cystines appear to play a role in stabilizing this preferred conformation of cycilc CPXC peptides. However. the distributions of backbone conformations and ${\beta}$-turns may indicate that the cyclic CPXC peptide seems to exist as an ensemble of ${\beta}$-turns and coiled conformations. The intirnsic stability of the cyclic CPXC motif itself the active conformation appears to play a role in determining electrochemical properties of disulfide oxidoreductases.

• Asian-Australasian Journal of Animal Sciences
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• 제8권2호
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• pp.119-122
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• 1995

A total of 6 tamaraws were observed for determining coat color and measured for body conformation. Banding pattern of 4 blood proteins and 2 isozymes were analysed from the peripheral blood of two tamaraws. The coat colour of younger tamaraws were observed to be brown and adult was found to be complete black. The body weight, body length, withers height, head length, head width, horn length and tail length of adult male and female tamaraws were: 236 kg and 208 kg; 113.5 cm and 112.5 cm; 19.5 cm and 20 cm; 30.0 cm and 28.5 cm and 36.0 cm and 35.5 cm, respectively. The electrophoretic banding pattern, distance migrated and the allelic frequencies obtained in tamaraws were similar compared with that reported in swamp buffaloes. Although the sample size was very small, results of this study could be an important source of informations based on which a breeding programme can be designed to exploit some of the economic characters of tamaraw.