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김종기,정진봉,백주열,이기암 단국대학교 신소재기술연구소 1993 신소재 Vol.3 No.-
DC Magnetron Sputtering 법으로 제조된 Ni_1-xFe_x 박막에 대해 박막의 두께 및 시편의 조성비가 자기저항비에 미치는 영향에 대하여 조사하였다. 시편의 조성비는 Fe chip의 개수로 조정하였으며, 박막의 두께는 400∼1600Å으로 변화시켰다. 복합타겟의 구성방법은 개량된 모자이크방식이었고, 자기저항비는 4-point probe를 이용하여 측정하였다. Fe의 조성이 증가함에 따라서 자기저항비는 증가하였으며, 조성이 x≒11에서 최대가 되었고, 두께가 증가함에 따라 자기저항비도 증가하였다. 제작된 모든 시편은 비정질구조를 나타내었다. We have investigated the magnetoresistance ratio on the influence of film thickness and range of sample composition about Ni_1-xFe_x Thin Film produced by DC Magnetron Sputtering. The range of sample composition was controlled by the number of Fe chips, and the range of deposited film was 400Å to 1600Å. Target formation was the improved mosaic type, and magnetoresistance ratio measured by 4-point probe method. The magnetoresistance ratio was increased with the increase of film thickness, and the magnetoresistance ratio was varied with sample composition. All samples were showed amorphous structure.
Human G-CSF synthesis using stress-responsive bacterial proteins.
Song, Jong-Am,Han, Kyung-Yeon,Park, Jin-Seung,Seo, Hyuk-Seong,Ahn, Keum-Young,Lee, Jeewon Published by Elsevier/North Holland on behalf of t 2009 FEMS microbiology letters Vol.296 No.1
<P>We previously reported that under the stress condition caused by the addition of 2-hydroxyethyl disulfide, a thiol-specific oxidant, to growing cultures of Escherichia coli BL21(DE3), a population of stress-responsive proteins [peptidyl-prolyl cis-trans isomerase B (PpiB), bacterioferritin (Bfr), putative HTH-type transcriptional regulator yjdC (YjdC), dihydrofolate reductase (FolA), chemotaxis protein cheZ (CheZ), and glutathione synthetase (GshB)] were significantly upregulated when compared with the nonstress condition. When those stress-responsive proteins were used as fusion partners for the expression of human granulocyte colony-stimulating factor (hG-CSF), the solubility of hG-CSF was dramatically enhanced in E. coli cytoplasm, whereas almost all of the directly expressed hG-CSF were aggregated to inclusion bodies. In addition, the spectra of circular dichroism measured with the purified hG-CSF were identical to that of standard hG-CSF, implying that the synthesized hG-CSF has native conformation. These results indicate that the bacterial stress-responsive proteins could be potent fusion expression partners for aggregation-prone heterologous proteins in E. coli cytoplasm.</P>
Song, Jong-Am,Lee, Dae-Sung,Park, Jin-Seung,Han, Kyung-Yeon,Lee, Jeewon Elsevier 2011 Enzyme and microbial technology Vol.49 No.2
<P><B>Abstract</B></P><P>Through the proteome analysis of <I>Escherichia coli</I> BL21(DE3), we previously identified the stress-responsive protein, arsenate reductase (ArsC), that showed a high cytoplasmic solubility and a folding capacity even in the presence of stress-inducing reagents. In this study, we used ArsC as an N-terminal fusion partner to synthesize nine aggregation-prone proteins as water-soluble forms. As a result, solubility of the aggregation-prone proteins increased dramatically by the fusion of ArsC, due presumably to its tendency to facilitate the folding of target proteins. Also, we evaluated and confirmed the efficacy of ArsC-fusion expression in making the fusion-expressed target proteins have their own native function or structure. That is, the self-assembly function of human ferritin light chain, <SMALL>L</SMALL>-arginine-degrading function of arginine deiminase, and the correct secondary structure of human granulocyte colony stimulating factor were clearly observed through transmission electron microscope analysis, colorimetric enzyme activity assay, and circular dichroism, respectively. It is strongly suggested that ArsC can be in general an efficient fusion expression partner for the production of soluble and active heterologous proteins in <I>E. coli</I>.</P>
Proteinticle Engineering for Accurate 3D Diagnosis
Lee, Jong-Hwan,Seo, Hyuk Seong,Song, Jong Am,Kwon, Koo Chul,Lee, Eun Jung,Kim, Ho Jin,Lee, Eun Bong,Cha, Young Joo,Lee, Jeewon American Chemical Society 2013 ACS NANO Vol.7 No.12
<P>In nature certain proteins are self-assembled inside cells to form nanoscale particles (named “proteinticles”) with constant structure and surface topology. Unlike chemically synthesized nanomaterials (<I>e.g</I>., various metal, carbon, and polymer nanoparticles), a variety of functional proteinticles can be easily created through genetic modification of the proteinticle surface, <I>i</I>.<I>e</I>., by adding or inserting specified proteins/peptides to the N- or C-terminus or the internal region of the protein constituent. Here we present proteins/peptides that recognize disease-specific antibodies on the surface of human ferritin based proteinticles for accurate 3D diagnosis of human autoimmune and infectious diseases. The surface display of the extracellular domain of myelin oligodendrocyte glycoprotein (MOG) with native conformation successfully discriminated between autoantibodies to native or denatured MOG, leading to the reliable diagnosis of multiple sclerosis with enhanced accuracy. Also we simultaneously displayed different antigenic peptides from hepatitis C virus (HCV) on the same proteinticle surface with modulating the composition of each peptide. The proteinticles with the heterogeneous peptide surface detected anti-HCV antibodies in patient sera with 100% accuracy. The proposed method of proteinticle engineering can be applied in general to the sensitive and specific diagnosis of many other human diseases.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/ancac3/2013/ancac3.2013.7.issue-12/nn404325t/production/images/medium/nn-2013-04325t_0005.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/nn404325t'>ACS Electronic Supporting Info</A></P>
Nam, Jong Woo,Park, Jun Young,Kim, Ji Hoon,Lee, Yong Soo,Lee, Eui Jong,Jeon, Min Jung,Kim, Hyung Soo,Jang, Am Balaban Publishers 2012 Desalination and Water Treatment Vol.43 No.1
<P> The osmotic backwash in the seawater reverse osmosis (SWRO) membrane induced by the osmotic pressure of a salt feed solution was investigated. The system was shifted immediately to a backwash process by reducing the operation pressure to zero to allow a net backwash driving force. The backwash process has two distinct stages: first stage-the backwash flux drops sharply at the initial, second stage-the backwash flux reaches equilibrium with time. A backwash cleaning efficiency is affected by some factors such as circulated water concentration, operation pressure, and cross-flow velocity in the SWRO membrane system combined with osmotic backwash. The feed water (or circulated water) concentration is the most influential and the pressure and cross-flow velocity are relatively less significant. In this study, the influence of backwashing water concentration on backwash cleaning efficiency was investigated under various circulated water concentrations. When the circulated water concentration was higher, the backwashing flux became greater and required less time to reach equilibrium; however, the internal concentration polarization occurred in the permeate side more rapidly and the backwash accumulated volume curve could be reversed with time. These results support the necessity of the optimization of the SWRO filtration/osmotic backwash mode between the concentrations of the feed water, the permeated and circulated water, and the time between the filtration and the backwash. </P>