• Smart Structures and Systems
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• 제25권4호
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• pp.423-432
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• 2020

In this paper, a novel but practical approach named series/parallel multi-sensing technique was proposed to evaluate the bolt looseness in a bolt group. The smart washers (SWs), which were fabricated by embedding a Lead Zirconate Titanate (PZT) transducer into two flat metal rings, were installed to the bolts group. By series connection of SWs, the impedance signals of different bolts can be obtained through only one sweep. Therefore, once the loosening occurred, the shift of different peak frequencies can be used to locate which bolt has loosened. The proposed multi input single output (MISO) damage detection scheme is very suitable for the structural health monitoring (SHM) of joint with a large number of bolts connection. Another notable contribution of this paper is the proposal of 3-dB bandwidth root mean square deviation (3 dB-RMSD) which can quantitatively evaluate the severity of bolt looseness. Compared with the traditional naked-eye observation method, the equivalent circuit based 3-dB bandwidth can accurately define the calculation range of RMSD. An experiment with three bolted connection specimens that installed the SWs was carried out to validate our proposed approach. Experimental result shows that the proposed 3 dB-RMSD based multi-sensing technique can not only identify the loosened bolt but also monitor the severity of bolt looseness.

• Bulletin of the Korean Chemical Society
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• 제25권12호
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• pp.1845-1849
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• 2004

Apolipoprotein B-100 (Apo-B100) is a major protein component for low density lipoproteins (LDL). A number of mimetic peptides of Apo-B100 were screened from the phase-displayed random peptide library by utilizing monoclonal antibody (B9). Mimetic peptide for B9 epitope against apo B-100 was CRNVPPIFNDVYWIAF (pB1). From the BLAST search, the mimetic peptide pB1 had 40% homology with apo B-100. 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 0.3-0.6 ${\AA}^2$ and the total RMSD was 0.5-1.5 ${\AA}. Moreover, pB1 structure included a weak $3_{10}$-helix from $Ile^7$,/TEX> to $Trp^{13}$.

• 한국자기공명학회논문지
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• 제20권3호
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• pp.95-101
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• 2016

Apolipoprotein B-100 (Apo-B100) is a major component of low density lipoprotein (LDL). Apo B-100 protein has 4,536 amino acid sequence and these amino acids are classified into peptide groups A to G with subsequent 20 amino acids (P1-P302). The peptide groups were act as immunoglobulin (Ig) antigens which oxidized via malondialdehyde (MDA). The mimetic peptide P1 (EEEMLENVSLVCPKDAT RFK) out of D-group peptides carrying the highest value of IgG antigens were selected for structural studies that may provide antigen specificity. Circular Dichroism (CD) spectra were measured for peptide secondary structure in the range of 190-250 nm. Experimental results show that P1 exhibit partial of ${\beta}-sheet$ and random coil structure. Homonuclear (COSY, TOCSY, NOESY) 2D-NMR experiments were carried out for NMR signal assignments and structure determination for P1. On the basis of these completely assigned NMR spectra and distance data, distance geometry (DG) and Molecular dynamics (MD) were carried out to determine the structures of P1. The proposed structure was selected by comparisons between experimental NOE spectra and back calculated 2D NOE results from determined structure showing acceptable agreement. The total Root-Mean-Square-Deviation (RMSD) value of P1 obtained upon superposition of all atoms was in the range $0.33{\AA}$. The solution state P1 has mixed structure of ${\beta}-sheet$ (Glu[1] to Cys[12]) and random coil (Pro[13] to Lys[20]). These NMR results are well consistent with secondary structure from experimental results of circular dichroism. Structural studies based on NMR may contribute to the studies of atherosclerosis and observed conformational characteristics of apo B-100 in LDL using monoclonal antibodies.