• 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.

• Kyungpook Mathematical Journal
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• v.56 no.3
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• pp.1003-1016
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• 2016

In this paper, we introduce a new kind of slant helix for null curves called null $W_n$-slant helix and we give a definition of new harmonic curvature functions of a null curve in terms of $W_n$ in (n + 2)-dimensional Lorentzian space $M^{n+2}_1$ (for n > 3). Also, we obtain a characterization such as: "The curve ${\alpha}$ s a null $W_n$-slant helix ${\Leftrightarrow}H^{\prime}_n-k_1H_{n-1}-k_2H_{n-3}=0$" where $H_n,H_{n-1}$ and $H_{n-3}$ are harmonic curvature functions and $k_1,k_2$ are the Cartan curvature functions of the null curve ${\alpha}$.

• 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.

• Journal of Microbiology and Biotechnology
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• v.26 no.10
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• pp.1701-1707
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• 2016

Lipoxygenase (LOX) is an industrial enzyme with wide applications in food and pharmaceutical industries. The available structure information indicates that eukaryotic LOXs consist of N terminus β-barrel and C terminus catalytic domains. However, the latest crystal structure of Pseudomonas aeruginosa LOX shows it is significantly different from those of eukaryotic LOXs, including the N-terminal helix domain. In this paper, the functions of this N-terminal helix domain in the soluble expression and catalysis of P. aeruginosa LOX were analyzed. Genetic truncation of this helix domain resulted in an insoluble P. aeruginosa LOX mutant. The active C-terminal domain was obtained by dispase digestion of the P. aeruginosa LOX derivative containing the genetically introduced dispase recognition sites. This functional C-terminal domain showed raised substrate affinity but reduced catalytic activity and thermostability. Crystal structure analyses demonstrate that the broken polar contacts connecting the two domains and the exposed hydrophobic substrate binding pocket may contribute to the insoluble expression of the C terminus domain and the changes in the enzyme properties. Our data suggest that the N terminus domain of P. aeruginosa LOX is required for its soluble expression in E. coli, which is different from that of the eukaryotic LOXs. Besides this, this N-terminal domain is not necessary for catalysis but shows positive effects on the enzyme properties. The results presented here provide new and valuable information on the functions of the N terminus helix domain of P. aeruginosa LOX and further improvement of its enzyme properties by molecular modification.

• The Journal of the Institute of Internet, Broadcasting and Communication
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• v.16 no.5
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• pp.229-233
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• 2016

In this paper, we present the four genetic nitrogenous bases of C, U(T), A, G to matrices and describe the structures from $4{\times}4$ RNA(ribose nucleic acid) to $8{\times}8$ DNA((deoxyribose nucleic acid) matrices. we analysis a deoxyribose nucleic acid (DNA) double helix based on the block circulant Hadamard-Jacket matrix (BCHJM). The orthogonal BCHJM is anti-symmetric pair complementary of the core DNA. The block circulant ribonucleic acid (RNA) repair damage reliability is better than the conventional double helix. In case of k=4 and N=1, the reliability of block circulant complementarity is 93.75%, and in case of k=4 and N=4, it is 98.44%. Therefore it improves 4.69% than conventional case of double helix.

• Journal of the Korean Magnetic Resonance Society
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• v.25 no.2
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• pp.17-23
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• 2021

High mobility group protein B1 (HMGB1) is a highly conserved, non-histone, chromatin associated nuclear protein encoded by HMGB1 gene. HMGB1 proteins may be general co-factors in Hox-mediated transcriptional activation that facilitate the access of Hox proteins to specific DNA targets. It is unclear that the exact binding interface of Hoxc9DBD and HMGB1. To identify the interface and binding affinity of Hoxc9DBD and HMGB1 A-box, the paramagnetic probe, MTSL was used in NMR titration experiment. It is attached to the N-terminal end of HMGB1 A-box by reaction with thiol groups. The backbone assignment of HMGB1 A-box was achieved with 3D NMR techinques. The ¹⁵N-labeled HMGB1 A-box was titrated with MTSL-labeled Hoxc9DBD respectively. Based on the chemical shift changes we can identify the interacting residues and further map out the binding sites on the protein structure. The NMR titration result showed that the binding interface of HMGB1 A-box is around loop-1 between helix-1 and helix-2. In addition, the additional contacts were found in N- and C-terminus. The N-terminal arm region of Hoxc9DBD is the major binding region and the loop between helix1 and helix2 is the minor binding region.

• Journal of the Korean Magnetic Resonance Society
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• v.19 no.2
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• pp.54-60
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• 2015

Papiliocin, from the swallowtail butterfly, Papilio xuthus, shows high bacterial cell selectivity against Gram-negative bacteria. Recently, we designed a 22mer analog with N-terminal helix from $Lys^3$ to $Ala^{22}$, PapN. It shows outstanding antimicrobial activity against Gram-negative bacteria with low toxicity against mammalian cells. In this study, we determined the 3-D structure of PapN in 300 mM DPC micelle using NMR spectroscopy and investigated the interactions between PapN and DPC micelles. The results showed that PapN has an amphipathic ${\alpha}$-helical structure from $Lys^3$ to $Lys^{21}$. STD-NMR and DOSY experiment showed that this helix is important in binding to the bacterial cell membrane. Furthermore, we tested antibacterial activities of PapN in the presence of salt for therapeutic application. PapN was calcium- and magnesium-resistant in a physiological condition, especially against Gram-negative bacteria, implying that it can be a potent candidate as peptide antibiotics.

• Journal of Photoscience
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• v.9 no.2
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• pp.114-117
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• 2002

Ultraviolet resonance Raman (UVRR) spectroscopy was used to elucidate the dynamic change of the protein structure of bacteriorhodopsin (BR) during the photocycle. The photointermediates minus light- adapted (LA) BR difference spectra show Trp difference signals, which are assigned to Trp189 or Trp182 on helix F by using the mutants, W182F and W189F. The Difference signals of Trp 182 indicates an increase in hydrogen bonding strength at the indole nitrogen and a large change in the side chain conformation (X$\^$2,1/ torsion angle) in the M$_1$ \longrightarrow M$_2$ transition. On the other hand, Trp189 shows an increased hydrophobic interaction. These results suggest that the tilt of helix F occurs in the M$_1$\longrightarrow M$_2$ transition. In the M$_2$ \longrightarrow N transition, the hydrophobic interaction of Trp182 decreases drastically, The decrease in hydrophobic interaction of Trp182 in the N state suggests an invasion of water molecules that promote the proton transfer from Asp96 to the Schiff base. Structural reorganization of the protein after the tilt of helix F may be important for efficient reprotonation of the Schiff base.

• The Korean Journal of Health Service Management
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• v.13 no.3
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• pp.81-92
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• 2019

Objectives: This study aimed to investigate the effects of auricular acupressure on anxiety and sleep among patients undergoing chemotherapy for breast cancer. Methods: A nonequivalent control group nonsynchronized design was employed. The experimental group received auricular acupressure on specific acupoints (shenmen, heart, kidney, subcortex), and the control group received auricular acupressure on helix 1, helix 2, helix 3, and helix 4 three times a day for three weeks. A total of 60 women were divided into an experimental (n=30) and control (n=30) group. Patient recruitment occurred between May and August 2019. The collected data were analyzed by a chi-square test, paired t-test, and independent t-tests using the SPSS 21.0 program. Results: There was a significant decrease in anxiety(t=4.61, p=<.001) and increase in sleep(t=3.81, p=<.001) in the experimental group compared to the control group. Conclusions: The findings confirm that auricular acupressure is an effective nursing intervention to decrease anxiety felt by patients undergoing chemotherapy and to increase the quality of their sleep.

• Molecules and Cells
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• v.21 no.3
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• pp.428-435
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• 2006

Specific interaction of the epsin N-terminal homology(ENTH) domain with the plasma membrane appears to bridge other related proteins to the specific regions of the membrane that are invaginated to form endocytic vesicles. An additional $\alpha$-helix, referred to as helix 0 (H0), is formed in the presence of the soluble ligand inositol-1,4,5-trisphosphate [$Ins(1,4,5)P_3$] at the N terminus of the ENTH domain (amino acid residues 3-15). The ENTH domain alone and full-length epsin cause tubulation of liposomes made of brain lipids. Thus, it is believed that H0 is membrane-inserted when it is coordinated with the phospholipid phosphatidylinositol-4,5-bisphosphate [$PtdIns(4,5)P_2$], resulting in membrane deformation as well as recruitment of accessory factors to the membrane. However, formation of H0 in a real biological membrane has not been demonstrated. In the present study, the membrane structure of H0 was determined by measurement of electron paramagnetic resonance (EPR) nitroxide accessibility. H0 was located at the phosphate head-group region of the membrane. Moreover, EPR line-shape analysis indicated that no pre-formed H0-like structure were present on normal acidic membranes. $PtdIns(4,5)P_2$ was necessary and sufficient for interaction of the H0 region with the membrane. H0 was stable only in the membrane. In conclusion, the H0 region of the ENTH domain has an intrinsic ability to form H0 in a $PtdIns(4,5)P_2$-containing membrane, perhaps functioning as a sensor of membrane patches enriched with $PtdIns(4,5)P_2$ that will initiate curvature to form endocytic vesicles.