• Proceedings of the Korean Society of Computer Information Conference
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• 2009.01a
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• pp.77-84
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• 2009

Intracellular signal transduction is achieved by protein-protein interaction. In this paper, we suggest performance algorithm based on Yeast protein-protein interaction and protein location information. We compare if pathways predicted with high valued weights indicate similar tendency with pathways provided in KEGG.

• BMB Reports
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• v.30 no.6
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• pp.410-414
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• 1997

We purified a protein carboxyl O-methyltransferase (protein methylase II) from porcine spleen to homogeneity. The molecular weight of the porcine spleen protein methylase II (ps-PM II) was estimated to be 27,500 daltons on SDS-PAGE. Amino acid sequence of N-terminal 28 residues for ps-PM II was identified. Amino-terminal three amino acid residues of ps-PM II were deleted when compared to those of other protein carboxyl methytransferase. S-Adenosyl-L-homocysteine competitively inhibits ps-PM II with a K, value of $1.63{\times}10^{-7}M$. Myelin basic protein exhibited the highest methyl-accepting capacity among the proteins tested.

• Biotechnology and Bioprocess Engineering:BBE
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• v.8 no.4
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• pp.263-267
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• 2003

Magnetic nanoparticles prepared from an alkaline solution of divalent and trivalent iron ions could covalently bind protein via the activation of Nethyl-N-(3-dimethylaminopropyl) carbodiimide (EDC). Trypsin and avidin were taken as the model proteins for the formation of protein-nanoparticle conjugates. The immobilized yield of protein increased with molar ratio of EDC/nanoparticie. Higher concentrations of added protein could yield higher immobilized protein densities on the particles. In contrast to EDC, the yields of protein immobilization via the a ctivation of cyanamide were relatively lower. Nanoparticles bound with avidin could attach a single-stranded DNA through the avidin-biotin interaction and hybridize with a DNA probe. The DNA hybridization was confirmed by fluorescence microscopy observations. Immobilized DNA on nanoparticles by this technique may have widespread applicability to the detection of specific nucleic acid sequence and targeting of DNA to particular cells.

• Korean Journal of Computational Design and Engineering
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• v.20 no.4
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• pp.321-327
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• 2015

In the protein database search, 3D structural shape comparison for protein screening plays a important role. Protein databases have big size and have been grown rapidly. Exhaustive search methods cannot provide a satisfactory performance. As protein is composed of a set of spheres, the similarity calculation of two set of spheres is very expensive. Thus, a reasonable filtering method could be an answer for the speedup of protein screening. In this paper, we suggest a speedup method for protein screening with atom number and bounding sphere. We also show some experimental results for the validity of our method.

• Korean Journal of Materials Research
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• v.28 no.3
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• pp.182-188
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• 2018

Nitrogen (N)-doped protein-based carbon as platinum (Pt) catalyst supports from tofu for oxygen reduction reactions are synthesized using a carbonization and reduction method. We successfully prepare 5 wt% Pt@N-doped protein-based carbon, 10 wt% Pt@N-doped protein-based carbon, and 20 wt% Pt@N-doped protein-based carbon. The morphology and structure of the samples are characterized by field emission scanning electron microscopy and transmission electron micro scopy, and crystllinities and chemical bonding are identified using X-ray diffraction and X-ray photoelectron spectroscopy. The oxygen reduction reaction are measured using a linear sweep voltammogram and cyclic voltammetry. Among the samples, 10 wt% Pt@N-doped protein-based carbon exhibits exellent electrochemical performance with a high onset potential of 0.62 V, a high $E_{1/2}$ of 0.55 V, and a low ${\Delta}E_{1/2}=0.32mV$. Specifically, as compared to the commercial Pt/C, the 10 wt% Pt@N-doped protein-based carbon had a similar oxygen reduction reaction perfomance and improved electrochemical stability.

• Biotechnology and Bioprocess Engineering:BBE
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• v.7 no.1
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• pp.26-30
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• 2002

A droplet fractionation method was previously developed to concentrate a dilute nonfoaming protein solution. In that earlier study with invertase, it was demonstrated that droplets created by ultrasonic energy waves could be enriched up to 8 times that of the initial dilute invertase solution. In this study, a mixture of bromelain (a foaming protein) and invertase (a nonfoaming protein) is investigated as a preliminary step to determine if droplet fractionation can also be used to separate a non-foaming protein from foaming proteins. The foaming mixture containing bromelain is first removed by bubbling the binary mixture with air. After the foam is removed, the protein rich air-water interfacial layer is skimmed off (prior to droplet fractionation) so as not to interfere with the subsequent droplet production from the remaining bulk liquid, rich in non-foaming protein. Finally, sonic energy waves are then applied to this residual bulk liquid to recover droplets containing the non-foaming protein, presumed to be invertase. The primary control variable used in this droplet fractionation process is the pH, which ranged for separate experiments between 2 and 9. It was observed that the maximum overall protein partition coefficients of 5 and 4 were achieved at pH 2 and 4, respectively, for the initial foaming experiment followed by the post foaming droplet fractionation experiment.

• Macromolecular Research
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• v.17 no.3
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• pp.192-196
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• 2009

Recently, the multi-screening of target materials has been made possible by the development of the surface plasmon resonance (SPR) imaging method. To adapt this method to biochemical analysis, the multi-patterning technology of protein microarrays is required. Among the different methods of fabricating protein microarrays, the microfluidic platform was selected due to its various advantages over other techniques. Microfluidic devices were designed and fabricated with polydimethylsiloxane (PDMS) by the replica molding method. These devices were designed to operate using only capillary force, without the need for additional flow control equipment. With these devices, multiple protein-patterned sensor surfaces were made, to support the two-dimensional detection of various protein-protein interactions with SPR. The fabrication technique of protein microarrays can be applied not only to SPR imaging, but also to other biochemical analyses.

• BMB Reports
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• v.34 no.2
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• pp.156-165
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• 2001

Leptin is a circulating non-glycosylated protein that is mainly produced in adipocytes. Leptin acts in the brain to regulate food intake and energy expenditure. Previously we reported our success in the isolation of a partial cDNA of the long form of the leptin receptor, OB-Rb, from rat spleen, and showed that leptin might also play a role in peripheral immune organs. In the present study, for the first time, the complete coding region of OB-Rb cDNA was cloned from rat splenocytes, and its nucleotide sequence was determined. The cDNA was then further expressed in E. coli and mammalian cells, thereby confirming the functional integrity of this receptor. Prokaryotically overexpressed OB-R protein was then used as an immunizing antigen in BALE/c mice to produce leptin receptor-specific antibodies. By using them, we confirmed the cell surface expression of OB-Rb in transfected CHO cells. It is our belief that the reagents, as produced in this study, will be of great use in further studies of the biological role of rat leptin.

• Biotechnology and Bioprocess Engineering:BBE
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• v.3 no.2
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• pp.82-86
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• 1998

The maltose binding protein (MBP) fusion protein system is a versatile tool to express and isolate recombinant proteins in E. coli. In this system, MBP fusion proteins are efficiently isolated from whole cell lysate using amylose conjugated agarose beads and then eluted by competition with free maltose. Since MBP is a rather large molecule (∼42 kDa), for further experiments, the MBP part is usually proteolytically cleaved from the fusion protein and subsequently removed by ion-exchange chromatography or rebinding to amylose columns after washing out excess and MBP-bound maltose. In the present study, we have developed an improved method for the removal of cleaved MBP, which is advantageous over conventional methods. In this method, factor Xa cleaved MBP fusion proteins were incubated with Sepharose beads conjugated with MBP specific monoclonal antibodies and then precipitated buy centrifugation, resulting in highly purified proteins in the supernatant.

• Journal of Microbiology and Biotechnology
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• v.12 no.5
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• pp.780-786
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• 2002

An immunosensor based on surface plasmon resonance (SPR) with a self-assembled protein G layer was developed for the detection of Escherichia coli O157:H7. A self-assembled protein C layer on a gold (Au) surface was fabricated by adsorbing the mixture of 11-mercaptoundecanoic acid (MUA) and hexanethiol at various molar ratios and by activating chemical binding between free amine (-$NH_2$) of protein G and 11-(MUA) using 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide hydrochloride (EDAC) in series. The formation of a self-assembled protein G layer on an Au substrate and the binding of the antibody and antigen in series were confirmed by SPR spectroscopy. The surface morphology analyses of the self-assembled protein G layer on the Au substrate, monoclonal antibody (Mab) against E. coli O157:H7 which was immobilized on protein G, and bound E. coli O157:H7 extracts on Immobilized Mab against E. coii O157:H7 were performed by atomic force microscopy (AFM). The detection limit of the SPR-based immunosensor for E. coli O157:H7 was found to be about $10^4$ cells/ml.