• Proceedings of the Korean Magnetic Resonance Society Conference
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• 1999.06a
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• pp.26-26
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• 1999

• Journal of the Korean Magnetic Resonance Society
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• v.12 no.2
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• pp.65-73
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• 2008

HP1298 (Swiss-Prot ID ; P65108) is an 72-residue protein from Helicobacter pylori strain 26695. The function of HP1298 was identified as Translation initiation factor IF-l based on sequence homology, and HP1298 is included in IF-l family. Here, we report the sequence-specific backbone resonance assignments of HP1298. About 97% of all the $^{1}HN$, $^{15}N$, $^{13}C{\alpha}$, $^{13}C{\beta}$, and $^{13}CO$ resonances could be assigned unambiguously. We could predict the secondary structure of HP1298, by analyzing the deviation of the $^{13}C{\alpha}$ and $^{13}C{\beta}$ shemical shifts from their respective random coil values. Secondary structure prediction shows that HP1298 consists of six $\beta$-strands. This study is a prerequisite for determining the solution structure of HP1298 and investigating the structure-function relationship of HP1298. Assigned chemical shift can be used for the study on interaction between HP1298 and other Helicobacter pylori proteins.

• Journal of the Korean Magnetic Resonance Society
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• v.18 no.1
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• pp.36-40
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• 2014

Predicting secondary structure of protein through assigned backbone chemical shifts has been used widely because of its convenience and flexibility. In spite of its usefulness, chemical shift based analysis has some defects including isotopic shifts and solvent interaction. Here, it is shown that corrected chemical shift analysis for secondary structure of protein. It is included chemical shift correction through consideration of deuterium isotopic effect and calculate chemical shift index using probability-based methods. Enhanced method was applied successfully to one of the proteins from Mycobacterium tuberculosis. It is suggested that correction of chemical shift analysis could increase accuracy of secondary structure prediction of protein and small molecule in solution.

• Journal of the Korean Magnetic Resonance Society
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• v.11 no.2
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• pp.73-84
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• 2007

MTH1821 (UniProtKB/TrEMBL ID O27849) is a 96-residue hypothetical protein from the open reading frame of Methanobacterium thermoautotrophicum H one of the target organisms of structural genomics pilot project. Proteins which contain conserved sequence compared with MTH1821 have not been discovered yet and the functional and structural information for MTH1821 is not available. Here, we present the sequence-specific backbone resonance using multidimensional heteronuc1ear NMR spectroscopy and propose the secondary structure using GetSBY software. The backbone resonances of N, HN, $C_{\alpha}$, $C_{\beta}$, CO and $H_{\alpha}$ which are necessary for a prediction of secondary structure by GetSBY were assigned about 98% (557/568). The secondary structure of MTH1821 confirmed that it is comprised of four strand regions and two helical regions. This report will provide a valuable resource for the calculation solution structure of MTH1821 and for the other hypothetical protein that is targeted for structural-based functional discovery.

• Journal of the Korean Magnetic Resonance Society
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• v.13 no.2
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• pp.117-125
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• 2009

HP0062 is an 86 residue hypothetical protein from Helicobacter pylori strain 26695. HP0062 was identified ESAT-6/WXG100 superfamily protein based on structure and sequence alignment and also contains leucine zipper domain sequence. Here, we report the sequence-specific backbone resonance assignment of HP0062. About 97.7% of all $^1H_N,\;^{15}N,\;^{13}C_{\alpha},\;^{13}C_{\beta}\;and\;^{13}C=O$ resonances were assigned unambiguously. We could predict the secondary structure of HP0062 by analyzing the deviation of the $^{13}C_{alpha}\;and\;^{13}C_{\beta}$ chemical shifts from their respective random coil values. Secondary structure prediction shows that HP0062 consist of two ${\alpha}$-helices. This study is a prerequisite for determining the solution structure of HP0062 and can be used for the study on interaction between HP0062 and DNA and other Helicobacter pylori proteins.

• Journal of the Korean Magnetic Resonance Society
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• v.19 no.1
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• pp.49-53
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• 2015

MRA1997 is a 76-residue conserved hypothetical protein of Mycobacterium tuberculosis H37Ra, one of the most pathogenic bacterial species and the causative agent of tuberculosis. In this study, the sequence-specific backbone resonance assignment of MRA1997 was performed using NMR spectroscopy. Approximately 88.3% of the total resonances could be unambiguously assigned. By analyzing deviations of the $C{\alpha}$ and $C{\beta}$ chemical shift values, the secondary structure of MRA1997 was calculated. The result revealed that secondary structure of MRA 1997 consists of one ${\alpha}$-helix and five ${\beta}$-sheets. Our structural study will be a footstone towards the characterization of the three-dimensional structure of MRA1997.

• Journal of the Korean Magnetic Resonance Society
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• v.16 no.2
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• pp.162-171
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• 2012

SAV2228 has an OB (Oligomer-Binding)-motif which is frequently used for nucleic acid recognition. To characterize the activity of translation initiation factor-1 (IF-1) from Staphylococcus aureus, SAV2228 was expressed and purified in Escherichia coli. We acquired 3D NMR spectra showing well dispersed and homogeneous signals which allow us to assign 94.4% of all $^1HN$, $^{15}N$, $^{13}C{\alpha}$, $^{13}C{\beta}$ and $^{13}CO$ resonances. We could predict a secondary structure of SAV2228 using TALOS and CSI from NMR data. SAV2228 was consisted of one ${\alpha}$-helix and five ${\beta}$-sheets. The predicted secondary structure, ${\beta}-{\beta}-{\beta}-{\alpha}-{\beta}-{\beta}$, was similar to other bacterial IF-1, but it was not completely same to the eukaryotic one. Assigned NMR peaks and secondary structre prediction can be used for the study on interaction with nucleic acid in the future.

• Journal of Power Electronics
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• v.17 no.6
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• pp.1391-1401
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• 2017

In this paper, a secondary resonance half-bridge dc-dc converter with an inductive output filter is presented. The primary side of such a converter utilizes asymmetric pulse width modulation (APWM) to achieve zero-voltage switching (ZVS) of the switches, and clamps the voltage of the switch to the input voltage. In addition, zero current switching (ZCS) of the output diode is achieved by a half-wave rectifier circuit with a filter inductor and a resonant branch in the secondary side of the proposed converter. Thus, the switching losses and diode reverse-recovery losses are eliminated, and the performance of the converter can be improved. Furthermore, an inductive output filter exists in the converter reduce the output current ripple. The operational principle, performance analysis and design equation of this converter are given in this paper. The analysis results show that the output diode voltage stress is independent of the duty cycle, and that the voltage gain is almost linear, similar to that of the isolation Buck-type converter. Finally, a 200V~380V input, 24V/2A output experimental prototype is built to verify the theoretical analysis.

• Journal of Power Electronics
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• v.14 no.6
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• pp.1224-1232
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• 2014

A full-bridge secondary dual-resonant DC-DC converter using the asymmetrical pulse-width modulated (APWM) strategy is proposed in this paper. The proposed converter achieves zero-voltage switching for the power switches and zero-current switching for the rectifier diodes in the whole load range without the help of any auxiliary circuit. Given the use of the APWM strategy, a circulating current that exists in a traditional phase-shift full-bridge converter is eliminated. The voltage stress of secondary rectifier diodes in the proposed converter is also clamped to the output voltage. Thus, the existing voltage oscillation of diodes in traditional PSFB converters is eliminated. This paper presents the circuit configuration of the proposed converter and analyzes its operating principle. Experimental results of a 1 kW 385 V/48 V prototype are presented to verify the analysis results of the proposed converter.

• Journal of Ocean Engineering and Technology
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• v.16 no.2
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• pp.27-31
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• 2002

The purpose of this study is to investigate the variation of resonance that is possible caused by construction of new port in a practical sea area between the existing port and the new one. The research of amplification that of the sea area was accomplished for the variation of resonance. In this study, long period wave that is observed continuously in the practical sea area was analyzed, and then secondary undulation was reproduced by numerical analysis. As a result of numerical analysis, the first mode resonant periods in the existing port is 640sec, and in the new one is 500sec. On the other hand, we know there is long period wave of 500sec from analyzation of field datas. Because that period this period is the resonant period in the new port. There is also the possibility of secondary undulation cause of resonant.