• 한국재료학회:학술대회논문집
• /
• 한국재료학회 1993년도 춘계학술발표회
• /
• pp.116-116
• /
• 1993

• 한국자기공명학회:학술대회논문집
• /
• 한국자기공명학회 2002년도 International Symposium on Magnetic Resonance
• /
• pp.38-39
• /
• 2002

• 한국자기공명학회논문지
• /
• 제4권1호
• /
• pp.41-49
• /
• 2000

To design more efficient peptide antagonist against the HBV, preSl(21-47) which carries the HBV receptor binding site for hepatocytes was synthesized and the solution structure of preSl(21-47) was investigated using CD spectroscopy and NMR spectroscopy in membrane-mimicking environments. According to CD spectra, preSl(21-47) has a random structure in aqueous solution, while conformational change was induced by addition of TFE and SDS micelle. Tertiary structures as determined by NMR spectroscopy shows that preSl(21-47) has a very flexible structure even in SDS micelle.

• 한국자기공명학회논문지
• /
• 제8권1호
• /
• pp.19-27
• /
• 2004

C-terminal fragments of APP (APP-CTs), that contain complete Abeta sequence, are found in neuritic plaques, neurofibrillary tangles and the cytosol of lymphoblastoid cells obtained from AD patients. CT16, Lys649-Asp664 (KKQYTSIHHGVVEVD) has been known as the most toxic part in the C-terminal fragment of amyloid precursor protein (APP). The solution structure of CT16 was investigated using NMR spectroscopy in various membrane-mimicking environments. According to Circular Dichroim (CD) spectra, CT16 has a random structure in aqueous solution, while conformational change was induced by addition of TFE and SDS micelle. Tertiary structure as determined by NMR spectroscopy shows that CT16 has a ${\beta}$-turn conformation in trifluoroethanol-containing aqueous solution.

• 한국자기공명학회논문지
• /
• 제21권2호
• /
• pp.50-54
• /
• 2017

Cupin-superfamily proteins represent the most functionally diverse groups of proteins and include a huge number of functionally uncharacterized proteins. Recently, YaiE, a cupin protein from Escherichia coli has been suggested to be involved in a novel activity of pyrimidine/purine nucleoside phosphorylase (PPNP). In the present study, we achieved a complete backbone NMR assignments of YaiE, by a series of heteronuclear multidimensional NMR experiments on its [$^{13}C/^{15}N$]-enriched sample. Subsequently, secondary structure analysis using the assigned chemical shift values identified 10 obvious ${\beta}-strands$ and a tentative $3_{10}-helix$. Taken all together, the results constitute the first structural characterization of a putative PPNP cupin protein.

• 한국응용약물학회:학술대회논문집
• /
• 한국응용약물학회 1996년도 춘계학술대회
• /
• pp.183-183
• /
• 1996

Bacteriophage T4 endonuclease V initiates the repair of ultraviolet (UV)-induced pyrimidine dimer photoproducts in duplex DNA. The mechanism of DNA strand cleavage involves four sequential stens: linear diffusion along dsDNA, pyrimidine dimer-specific binding,l pyrimidine dimer-DNA glycosylase activity, and Af lyase activity. Although crystal structure is known for this enzyme, solution structure has not been yet known. In order to elucidate the solution structure of this enzyme NMR spectroscopy was used. As a basis for the NMR peak assignment of the protein, HSQC spectrum was obtained on the uniformly $\^$15/N-labeled T4 endonuclease V. Each amide peak of the spectrum were classified according to amino acid spin systems by interpreting the spectrum of $\^$15/N amino acid-specific labeled T4 endonuclease V. The assignment was mainly obtained from three-dimensional NMR spectra such as 3D NOESY-HMQC, 3D TOCSY-HMQC. These experiments were carried out will uniformly $\^$15/N-labeled sample. In order to assign tile resonance of backbon atom, triple-resonance theree-dimensional NMR experiments were also performed using double labeled($\^$15/N$\^$13/C) sample. 3D HNCA, HN(CO)CA, HNCO, HN(CA)HA spectra were recorded for this purpose. The results of assignments were used to interpret the interaction of this enzyme with DNA. HSQC spectrum was obtained for T4 endonuclease V with specific $\^$15/N-labeled amino acids that have been known for important residue in catalysis. By comparing the spectrum of enzyme*DNA complex with that of the enzyme, we could confirm the important role of some residues of Thr, Arg, Tyr in activity. The results of assignments were also used to predict the secondary structure by chemical shift index (CSI).

• 공업화학
• /
• 제4권4호
• /
• pp.770-775
• /
• 1993

에틸렌글리콜과 1, 4-시클로헥산디메탄올의 테레프탈산 공중합체인, poly(ethylene terephthalate-co-1, 4-cyelohexylene dimethylene terephthalate), P(ET-CT)의 화학 구조를 고분해능 NMR 분석을 통하여 조사하였다. $^1H$ NMR 분석에서 메칠렌기에 의한 chemical shift가 ET, 트란스 CT, 및 시스 CT로 분리됨에 따라 공중합조성 및 이성질체의 비율을 구할 수 있었다. $^{13}C$ NMR 분석에서 카르보닐기에 연결된 벤젠기의 탄소가 diad로 분리됨에 따라 공중합 연쇄 분포(copolymer sequence distribution)를 구한 결과, P(ET-CT) 공중합체는 랜덤공중합체임이 판명되었다. 아울러 랜덤 통계식을 이용하여 공중합 연쇄의 분포 및 평균길이를 구할 수 있었다.

• 한국신재생에너지학회:학술대회논문집
• /
• 한국신재생에너지학회 2005년도 춘계학술대회
• /
• pp.615-617
• /
• 2005

[ $^{13}C$ ] NMR spectra were obtained for pure $CH_4$ hydrate in order to identify hydrate structure and cage occupancy of guest molecule. The NMR technique can provide both qualitative and quantitative hydrate characteristics. The moles of methane captured into pure $CH_4$ hydrate per mole of water were found to be similar to the full occupancy value. The overall results drawn from this study can be usefully applied to storage and transportation of natural gas.

• Bulletin of the Korean Chemical Society
• /
• 제32권11호
• /
• pp.4016-4020
• /
• 2011

A number of mimetic peptides of apolipoprotein A-I, a major component for high density lipoproteins (HDL), were screened from the phase-displayed random peptide library by utilizing monoclonal antibodies (A12). A mimetic peptide for A12 epitope against apolipoprotein A-I was selected as FVLVRDTFPSSVCCP(pA2) exhibiting 45% homology with Apo A-I in the BLAST search. Solution structure determination of this mimotope was made by using 2D-NMR data and NMR-based distance geometry (DG)/molecular dynamic calculations. The resulting DG structures had low penalty value of 0.4-0.6 ${\AA}^2$ and the total RMSD of 0.7-1.7 ${\AA}$. The mimotope pA2 exhibited a characteristic ${\beta}$-turn conformation from Val[2] to Phe[8] near Pro[9] residue.

• Bulletin of the Korean Chemical Society
• /
• 제32권9호
• /
• pp.3425-3428
• /
• 2011

Apolipoprotein A-I (Apo A-I) is a major component for high density lipoproteins (HDL). A number of mimetic peptides of Apo A-I were screened from the phase-displayed random peptide library by utilizing monoclonal antibodies (A12). Mimetic peptide for A12 epitope against Apo A-I was selected as CPFARLPVEHHDVVGL (pA1). From the BLAST search, the mimetic peptide pA1 had 40% homology with Apo A-I. As a result of the structural determination of this mimotope using homo/hetero nuclear 2D-NMR techniques and NMR-based distance geometry (DG)/molecular dynamic (MD) computations, DG structure had low penalty value of 0.3-0.7 ${\AA}^2$ and the total RMSD was 0.6-1.6 ${\AA}$. The mimotope pA1 exhibited characteristic conformation including a ${\beta}$-turn from Pro[7] to His[11].