6 results match your criteria Bulletin Of The Korean Chemical Society[Journal]

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Pump-Probe X-ray Solution Scattering Reveals Accelerated Folding of Cytochrome Upon Suppression of Misligation.

Bull Korean Chem Soc 2014 Mar;35(3):695-696

Department of Chemistry, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 305-701, Korea ; Center for Nanomaterials and Chemical Reactions, Institute for Basic Science (IBS), Daejeon 305-701, Korea.

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http://dx.doi.org/10.5012/bkcs.2014.35.3.697DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4072328PMC
March 2014
11 Reads

Dosage Effects of Salt and pH Stresses on as Monitored Metabolites by Using Two Dimensional NMR Spectroscopy.

Bull Korean Chem Soc 2013 Dec;34(12):3602-3608

Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.

, which is a common species of yeast, is by far the most extensively studied model of a eukaryote because although it is one of the simplest eukaryotes, its basic cellular processes resemble those of higher organisms. In addition, yeast is a commercially valuable organism for ethanol production. Since the yeast data can be extrapolated to the important aspects of higher organisms, many researchers have studied yeast metabolism under various conditions. Read More

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http://dx.doi.org/10.5012/bkcs.2013.34.12.3602DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4311725PMC
December 2013
6 Reads

Tracing Metabolite Footsteps of Along the Time Course of Recombinant Protein Expression by Two-Dimensional NMR Spectroscopy.

Bull Korean Chem Soc 2012 Dec;33(12):4041-4046

Department of Chemistry and Institute for Chemical Biology, Sejong University, Seoul 143-747, Korea.

The recombinant expression of proteins has been the method of choice to meet the demands from proteomics and structural genomics studies. Despite its successful production of many heterologous proteins, failed to produce many other proteins in their native forms. This may be related to the fact that the stresses resulting from the overproduction interfere with cellular processes. Read More

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3686544PMC
December 2012
4 Reads

Role of diffusion in the kinetics of reversible enzyme-catalyzed reactions.

Bull Korean Chem Soc 2012 6;33(3):925-928. Epub 2012 Jan 6.

Laboratory of Chemical Physics, National Institute of Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.

The accurate expression for the steady-state velocity of an irreversible enzyme-catalyzed reaction obtained by Shin and co-workers is generalized to allow for the rebinding of the product. The amplitude of the power-law (t(-1/2)) relaxation of the free- and bound-enzyme concentrations to steady-state values is expressed in terms of the steady-state velocity and the intrinsic (chemical) rate constants. This result is conjectured to be exact, even though our expression for the steady-state velocity in terms of microscopic parameters is only approximate. Read More

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http://dx.doi.org/10.5012/bkcs.2012.33.3.925DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3571119PMC
January 2012
2 Reads

Synthesis and Binding Affinity of Homologated Adenosine Analogues as A Adenosine Receptor Ligands.

Bull Korean Chem Soc 2011;32(5):1620-1624

Department of Bioinspired Science and Laboratory of Medicinal Chemistry, College of Pharmacy, Ewha Womans University, Seoul 120-750, Korea.

Homologated analogues and of potent and selective A adenosine receptor ligands, IB-MECA and dimethyl-IB-MECA were synthesized from commercially available 1--acetyl-2,3,5-tri--benzoyl-β-d-ribofuranose () Co(CO)-catalyzed siloxymethylation as a key step. Unfortunately, homologated analogues and did not show significant binding affinities at three subtypes of adenosine receptors, indicating that free rotation, resulting from homologation, induced unfavorable interactions in the binding site of the receptor maybe due to the presence of many conformations. Read More

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http://dx.doi.org/10.5012/bkcs.2011.32.5.1620DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4478603PMC
January 2011

Recombinant Expression, Isotope Labeling and Purification of the Vitamin D Receptor Binding Peptide.

Bull Korean Chem Soc 2011 ;32(12):4337-4340

Department of Chemistry and Institute for Chemical Biology, Sejong University, Seoul 143-747, Korea ; Department of Biochemistry, University of Wisconsin - Madison, Madison, WI 53706, USA.

The vitamin D receptor binding peptide, VDRBP, was overexpressed as a fused form with the ubiquitin molecule in Rosetta(DE3)pLysS, a protein production strain of harboring an induction controller plasmid. The fusion protein was bound to the immobilized metal ions, and the denaturation and renaturation of the fusion protein were performed as a part of the purification procedure. After the elution of the fusion protein, the peptide hormone was released from its fusion partner by using yeast ubiquitin hydrolase (YUH), and subsequently purified by reverse phase chromatography. Read More

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http://dx.doi.org/10.5012/bkcs.2011.32.12.4337DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3634580PMC
January 2011
2 Reads
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