• Journal of the Korean Chemical Society
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• v.31 no.5
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• pp.471-475
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• 1987

Fe(II)-poly(D-glutamic acid) (PGA) complex in aqueous solution has been investigated as functions of pH and concentration of Fe(II) by using absorption and circular dichroism spectroscopies. The helix-breaking interaction occurred at pH 4.3 while the helix-directing one occurred at pH 5.7 after forming complex between PGA and Fe(II). The relationship between conformation change of PGA by forming complex with Fe(II) and complex constants for the above system was studied. As a result, stability constants in random coil structure of PGA are larger than those in ${\alpha}$-helix structure. This result indicates that the random coil structure of PGA-Fe(II) complex shows more stable complex than ${\alpha}$-helix one.

• Proceeding of EDISON Challenge
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• 2016.03a
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• pp.75-79
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• 2016

A helical nanosturctrue can be obtained by self-assembly method. Utilizing DPD simulation coarse-grained model, we patterned 2D layer nanosheets with repeated diagonal defects and grafts, and programed to self-roll into hollow helix structure. The defected pattern side caused anisotropy, and formed helix or helix-like structure. This opens the possibility to control the helix pitch or cavity radius. In this work, we designed several patterns about diagonal defect with a variety of defect side densities and defect widths and then simulation was carried out. Thus, our results have that parameters are affecting self-assembly of nanosheets and their conformation.

• Bulletin of the Korean Chemical Society
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• v.19 no.1
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• pp.57-62
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• 1998

We have synthesized a 17-residue peptide with the amino acid sequence RQMKEDAKGKSEEELAD corresponding to residues 84-100 of chicken skeletal troponin C. This stretch of the protein sequence is in the middle one-third of the 32-residue 9-turn α-helix that connects the two globular domains of the dumbell-shaped molecule and includes the D/E linker helix. We describe here the solution conformation of the helix linker as studied by circular dichroism (CD) and two-dimensional nuclear magnetic resonance (2-D NMR) spectroscopy. The NOE connectivities together with the vicinal $^3J_{N{\alpha}}$ coupling constants suggest that the peptide exists in a fast conformational equilibrium among several secondary structure: a nascent helix near the N-terminus, a helix, and a substational population of extended and random coil forms. In addition, two interresidue α-α NOEs are observed suggesting a bent structure with a bend that includes the single glycine in position 92. These results are consistent with the ideas that in neutral solution the D/E linker region of the central helix in troponin C can adopt a helical conformation and the central helix may have a segmental flexibility around Gly 92.

• Molecules and Cells
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• v.42 no.10
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• pp.729-738
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• 2019

Autophagy is an important process for protein recycling. Oligomerization of p62/SQSTM1 is an essential step in this process and is achieved in two steps. Phox and Bem1p (PB1) domains can oligomerize through both basic and acidic surfaces in each molecule. The ZZ-type zinc finger (ZZ) domain binds to target proteins and promotes higher-oligomerization of p62. This mechanism is an important step in routing target proteins to the autophagosome. Here, we determined the crystal structure of the PB1 homo-dimer and modeled the p62 PB1 oligomers. These oligomer models were represented by a cylindrical helix and were compared with the previously determined electron microscopic map of a PB1 oligomer. To accurately compare, we mathematically calculated the lead length and radius of the helical oligomers. Our PB1 oligomer model fits the electron microscopy map and is both bendable and stretchable as a flexible helical filament.

• Proceedings of the Korean Society for Bioinformatics Conference
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• 2000.11a
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• pp.86-87
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• 2000

Protein folding is a fundamental problem in structural bioinformatics and so numerous studies have been devoted to the subject. As the most common regular secondary conformation in proteins, helix has been an important ingredient of the protein folding problem. In particular, alanine based polypeptides are widely studied to identify the helix folding process in that the aianine amino acid is known to have one of the highest helix propensities. In principle, intrinsic helix propensities can be obtained from gas-phase measurements where solvent effect is absent. Hudgins et al. studied alanine-based peptides in vacuo using high-resolution ion mobility measurement technique. It was reported that introduction of a single Iysine at the C terminus resulted in the formation of very stable, monomeric polyalanine helices. We also have investigated helix formation in vacuo with different terminal charge conditions; we have found a new type of helix motif, To the best of our knowledge, this type of helix conformation has not been characterized before and we name it as I-helix.

• Proceedings of the KIEE Conference
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• 2008.04a
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• pp.145-150
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• 2008

This paper suggests an applicable study on Helix TWT of Slow-Wave Structure for Surveillance RADAR. In order to improve Slow-Wave Structure performance and analysis, we design and realizer a Helix TWTA using a HFSS Code and LMSuite Code, Through the cutting and simulation of Helix TWTA, this parameter satisfies the design specifications, Therefore, this specifics is very useful and can be used to develop the similar equipments.

• Proceedings of the Korean Biophysical Society Conference
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• 2003.06a
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• pp.58-58
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• 2003

The envelope glycoprotein of HIV, gp41, mediates the membrane fusion with human cells. The extracellular domain of gp41 has two helical regions. The N-terminus helical region (N-helix) forms trimeric coiled coil, interacts with the C-terminus helical region (C-helix) of gp41 to form a stable helical bundle structure. In this study, we have shown that the N-helix of gp41 has membrane interacting and disrupting abilities. It was localized into the interface of the lipidic phase and head group of the membrane. In contrast, the N-helix region with membrane fusion defective mutations could not bind to membrane. In addition, the N-helix bound on the membrane was released from the membrane by the C-helix, and the complex of the N- and C-helix did not interact with membrane. These results suggested that the membrane binding ability of the N-helix is necessary for the fusion activity of gp41, and such property is possibly controlled by the C-helm.

• Journal of the Korean Magnetic Resonance Society
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• v.19 no.3
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• pp.149-155
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• 2015

Acyl carrier protein is related with fatty acid biosynthesis in which specific enzymes are involved. Especially, acyl carrier protein (ACP) is the key component in the growing of fatty acid chain. ACP is the small, very acidic protein that covalently binds various intermediates of fatty acyl chain. Acylation of ACP is mediated by holo-acyl carrier protein synthase (ACPS), which transfers the 4'PP-moiety of CoA to the 36th residue Ser of apo ACP. Acyl carrier protein P (ACPP) is one of ACPs from Helicobacter plyori. The NMR structure of ACPP consists of four helices, which were reported previously. Here we show how acylation of ACPP can affect the overall structure of ACPP and figured out the contact surface of ACPP to acyl chain attached during expression of ACPP in E. coli. Based on the chemical shift perturbation data, the acylation of ACCP seems to affect the conformation of the long loop connecting helix I and helix II as well as the second short loop connecting helix II and helix III. The significant chemical shift change of Ile 54 upon acylation supports the contact of acyl chain and the second loop.

• Journal of Microbiology and Biotechnology
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• v.9 no.5
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• pp.562-567
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• 1999

Single-stranded DNA binding protein (SSB) is well-characterized as having a helix-destabilizing activity. The helix-destabilizing capability of SSB has been re-examined in this study. The results of restriction endonuclease protection assays and titration experiments suggest that the stimulatory effect of SSB on strand exchange acts by melting out the secondary structure which is inaccessible to RecA protein binding; however, SSB is excluded from regions of secondary structure present in native single-stranded DNA. Complexes of SSB and RecA protein are required for eliminating the secondary structure barriers under optimal conditions for strand exchange.

• Journal of Engineering Education Research
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• v.21 no.6
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• pp.54-62
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• 2018

This study is an analysis of the process of the discovery of the DNA double helix structure from an engineering literacy education perspective. The explanation of the DNA double helix structure by James Watson and Francis Crick in 1952 is a well-known scientific episode. The process is also a combination of various incidents that can frequently happen in competitive engineering research and development situations. Therefore, the process of the discovery of the DNA structure is a remarkable event that can cover all subjects, such as engineering and ethics, research ethics, communication between researchers, engineering and leadership, engineering and teamwork, and engineering and women. This paper focuses on analyzing the research ethics issues associated with Rosalind Franklin and comparing and analyzing the three teams that were very close to the discovery of the DNA structure. By looking at why the Watson and Crick team got the final answer instead of the Linus Pauling's team or the Maurice Wilkins and Rosalind Franklin's team, the virtues of the technology development process that should be taught in engineering literacy education will be naturally presented.