http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
Nian, Rui,Kim, Duck Sang,Nguyen, Thuong,Tan, Lihan,Kim, Chan-Wha,Yoo, Ik-Keun,Choe, Woo-Seok Elsevier 2010 Journal of chromatography Vol.1217 No.38
<P><B>Abstract</B></P><P>Toxic heavy metal pollution is a global problem occurring in air, soil as well as water. There is a need for a more cost effective, renewable remediation technique, but most importantly, for a recovery method that is selective for one specific metal of concern. Phage display technology has been used as a powerful tool in the discovery of peptides capable of exhibiting specific affinity to various metals or metal ions. However, traditional phage display is mainly conducted in batch mode, resulting in only one equilibrium state hence low-efficiency selection. It is also unable to monitor the selection process in real time mode. In this study, phage display technique was incorporated with chromatography procedure with the use of a monolithic column, facilitating multiple phage-binding equilibrium states and online monitoring of the selection process in search of affinity peptides to Pb<SUP>2+</SUP>. In total, 17 candidate peptides were found and their specificity toward Pb<SUP>2+</SUP> was further investigated with bead-based enzyme immunoassay (EIA). A highly specific Pb<SUP>2+</SUP> binding peptide ThrAsnThrLeuSerAsnAsn (TNTLSNN) was obtained. Based on our knowledge, this is the first report on a new chromatographic biopanning method coupled with monolithic column for the selection of metal ion specific binding peptides. It is expected that this monolith-based chromatographic biopanning will provide a promising approach for a high throughput screening of affinity peptides cognitive of a wide range of target species.</P>
Nian, Rui,Kim, Duck Sang,Tan, Lihan,Kim, Chan-Wha,Choe, Woo-Seok Wiley (John WileySons) 2009 Biotechnology progress Vol.25 No.4
<P>The use of polyethylene glycol (PEG) as a refolding additive to a refolding cocktail comprising the molecular bichaperone ClpB and DnaKJE significantly enhances chaperone-mediated refolding of heat-denatured malate dehydrogenase (MDH). The critical factor to affect the refolding yield is the time point of introducing PEG to the refolding cocktail. The refolding efficiency reached approximately 90% only when PEG was added at the beginning of refolding reaction. The synergistic coordination of an inexpensive refolding additive PEG with the ClpB/DnaKJE bichaperone system may provide an economical route to further enhance the efficacy of ClpB/DnaKJE refolding cocktail approach, facilitating its implementation in large-scale refolding processes.</P>
Kim, Jung Kyu,Jang, Ji-ryang,Salman, Muhammad Saad,Tan, Lihan,Nam, Chang-Hoon,Yoo, Pil J.,Choe, Woo-Seok Elsevier 2019 Ceramics international Vol.45 No.5
<P><B>Abstract</B></P> <P>Biomineralization is a promising material synthesis strategy for environmentally benign production of nanostructured metal oxides. An important question is whether biomineralization can be used in the biomimetic synthesis of TiO<SUB>2</SUB> with tunable photocatalytic properties that are conducive to diverse solar energy conversion applications. Here, we report the biomineralization of energy-state-modified TiO<SUB>2</SUB> nanoparticles, where the critical properties closely related to their photocatalytic activity can be manipulated by tailoring the nature of the designer biotemplates. For this purpose, STB1 heptapeptide was employed as a nucleation center to induce TiO<SUB>2</SUB> biomineralization. Three distinctive types of biomolecules (peptide, protein, and phage) were deliberately designed to contain the STB1 nucleation core at different local densities and intermolecular distances. The degree of substitutional nitrogen-doping and the morphology are all subject to the context-dependent differential availability of STB1 in the biomineralization milieu. Phage-induced biomineralization results in TiO<SUB>2</SUB> with modified energy state and wire-like network morphology, which account for significantly enhanced charge dissociation/transport performance and high photocatalytic activity. This is the first study to report that a specific peptide with biomineralizing activity exerts differential impacts on the properties of resulting biomineralization products in a context-dependent manner, and will provide a powerful new strategy for tailoring of material properties via biomineralization.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Biomimetic synthesis of TiO<SUB>2</SUB> with tunable photochemical properties. </LI> <LI> Deliberately designed peptide, protein, and phage to contain the STB1 nucleation core. </LI> <LI> Synchronized control of size, morphology, and substitutional nitrogen-doping. </LI> <LI> Modification of the energy states for efficient photocatalytic activity. </LI> </UL> </P> <P><B>Graphical abstract</B></P> <P>[DISPLAY OMISSION]</P>
Jang, Sung Kyu,Kim, Sookyung,Salman, Muhammad Saad,Jang, Ji-ryang,Um, Yu Mi,Tan, Lihan,Park, Jin-Hong,Choe, Woo-Seok,Lee, Sungjoo American Chemical Society 2018 Chemistry of materials Vol.30 No.3
<P>A high-performance biomaterial-based resistive switching (RS) device is fabricated by harnessing a thermally denatured protein (hexa-His-tagged recombinant molecular chaperone DnaJ (rDnaJ)) as a switching layer in a Cu/rDnaJ/Pt configuration on SiO<SUB>2</SUB>/Si substrate. The conductivity of the heat-denatured rDnaJ protein layer between the metal electrodes can be reversibly controlled to enable the formation/rupture of conductive Cu filaments by tailoring the metal chelating properties of the amino acid residues in the insulating protein matrix in a pH- and/or redox potential-dependent manner, giving rise to high-performance nonvolatile RS behavior. The rDnaJ-based RS device exhibits extremely low set voltage (∼0.12 V) and reset voltage (∼−0.08 V) with excellent uniformity, along with large memory window (<I>R</I><SUB>HRS</SUB>/<I>R</I><SUB>LRS</SUB> > 10<SUP>6</SUP>) and long retention time (>10<SUP>6</SUP> s). In addition, the rDnaJ RS device, which is fabricated on a flexible poly(ethylene terephthalate) substrate, exhibits an uncompromised switching performance. The present study is the first attempt to explore the use of a recombinant protein as a functional switching layer in RS devices. This approach opens up a new method of harnessing recombinant proteins with engineered properties as powerful building blocks to suit the requirements of next-generation biocompatible, flexible, high-performance, and low power consumption electronics.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/cmatex/2018/cmatex.2018.30.issue-3/acs.chemmater.7b04261/production/images/medium/cm-2017-04261p_0004.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/cm7b04261'>ACS Electronic Supporting Info</A></P>