• Title/Summary/Keyword: Biophysics

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Comparative Analyses of Commercial Detonation Nanodiamonds

  • Puzyr, A.P.;Burova, A.E.;Bondar, V.S.;Rhee, C.K.;Rhee, W.H.;Hwang, K.C.
    • Journal of Powder Materials
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    • v.18 no.3
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    • pp.297-302
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    • 2011
  • Colloidal stability is one of crucial factors for many applications of nanodiamond. Despite recent development, nanodiamonds available on the market often exhibit a high impurity content, wide size distribution of aggregates and low resistance to sedimentation. In the current study, four commercial nanodiamond powders synthesized by detonation synthesis were surface modified and then separated with respect to the size into six fractions by centrifugation. The fractions were evaluated by zeta potential, particle size distribution and elemental composition. The results showed that the modified nanodiamonds form stable colloidal suspensions without sedimentation for a long time.

Adsorptive Immobilization of Acetylcholine Esterase on Octadecyl Substituted Porous Silica: Optical Bio-analysis of Carbaryl

  • Norouzy, Amir;Habibi-Rezaei, Mehran;Qujeq, Durdi;Vatani, Maryam;Badiei, Alireza
    • Bulletin of the Korean Chemical Society
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    • v.31 no.1
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    • pp.157-161
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    • 2010
  • A sensory element against carbaryl, as a widely used pesticide was prepared based on adsorbed acetylcholine esterase (AChE) from Torpedo california. Octadecyl was substituted on macro-porous silica, confirmed by infra-red (IR) spectroscopy and quantitatively estimated through thermo-gravimetric analysis (TGA). Immobilization of the enzyme was achieved by adsorption on this support. Activity of the immobilization product was measured as a function of the loaded enzyme concentration, and maximum binding capacity of the support was estimated to be 43.18 nmol.mg-1. The immobilized preparations were stable for more than two months at storage conditions and showed consistency in continuous operations. Possible application of the immobilized AChE for quantitative analysis of carbaryl is proposed in this study.

A New Approach for Thermodynamic Study on the Binding of Human Serum Albumin with Cerium Chloride

  • Rezaei Behbehani, G.;Divsalar, A.;Saboury, A.A.;Faridbod, F.;Ganjali, M.R.
    • Bulletin of the Korean Chemical Society
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    • v.30 no.6
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    • pp.1262-1266
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    • 2009
  • Thermodynamics of the interaction between Cerium (III) chloride, $Ce^{3+}$, with Human Serum Albumin, HSA, was investigated at pH 7.0 and $27\;{^{\circ}C}$ in phosphate buffer by isothermal titration calorimetry. Our recently solvation model was used to reproduce the enthalpies of HSA interaction by $Ce^{3+}$. The solvation parameters recovered from our new model, attributed to the structural change of HSA and its biological activity. The interaction of HSA with $Ce^{3+}$ showed a set of two binding sites with negative cooperativity. $Ce^{3+}$ interacts with multiple sites on HSA affecting its biochemical and biophysical properties.

In Vivo Quantitative Analysis of PKA Subunit Interaction and cAMP Level by Dual Color Fluorescence Cross Correlation Spectroscopy

  • Park, Hyungju;Pack, Changi;Kinjo, Masataka;Kaang, Bong-Kiun
    • Molecules and Cells
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    • v.26 no.1
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    • pp.87-92
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    • 2008
  • We employed dual color Fluorescence Cross Correlation Spectroscopy (FCCS) to measure the interaction between PKA regulatory (RII) and catalytic subunits (CAT) in living cells. Elevation of intracellular cAMP with forskolin decreased the cross-correlation amplitude between RFP-fused RII (RII -mRFP) and GFP-fused CAT (CAT-EGFP) by 50%, indicating that cAMP elevation leads to dissociation of RII-CAT complexes. Moreover, diffusion coefficient analysis showed that the diffusion rate of CAT-EGFP was significantly increased, suggesting that the decreased RII-CAT association caused by cAMP generated free CAT subunits. Our study demonstrates that in vivo FCCS measurements and their quantitative analysis permit one not only to directly quantify protein-protein interactions but also to estimate changes in the intracellular cAMP concentration.

PYRANOSE OXIDASE HAVING A COVALENTLY BOUND FAD AS A COENZYME

  • Kwon, Jae-Youl;Kang, Sa-Ouk
    • Proceedings of the Korean Biophysical Society Conference
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    • 1996.07a
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    • pp.45-45
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    • 1996
  • Flavin-peptides were purified from pyranose oxidase (EC 1.1.3.10) after tryptic- chymotryptic and tryptic digestion. The spectral and chromatographic properties of these flavin peptides showed that the FAD of pyranose oxidase appears to be bound, by way of the 8${\alpha}$-methylene group, to the N-l position of the imidazole ring of the histidine. Automated sequence analysis showed that the amino acid sequence of the tryptic-chymotryptic flavin-peptide from pyranose oxidase is Ser-Thr-X-Trp and that of the tryptic flavin-peptide is Met-Ser-Thr-X-Trp. (omitted)

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Structural Characteristics of NiSOD from Streptomyces seoulensis

  • Lee, Jin-Won;Wuerges, Jochen;Carugo, Kristina Djinovic;Kang, Sa-Ouk
    • Proceedings of the Korean Biophysical Society Conference
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    • 2002.06b
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    • pp.50-50
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    • 2002
  • The heterologous expression of sodN gene from Streptomyces seoulensis in Streptomyces lividans together with the gel filtration and sedimentation equilibrim data indicated that the quaternary structure of NiSOD is homohexamer, which is novel among SODs, not the previously reported homotetramer. The EPR spectrum of $^{61}$ Ni (I = 3/2) substituted NiSOD showed a clear resolved hyperfine structure at g=2.016, unambiguously identifying that the EPR signal from NiSOD is due to Ni.(omitted)

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Nickel Binding Protein (NBPI) and Its Gene from Streptomyces seoulensis

  • Kim, In-Kwon;Sa-Ouk kang
    • Proceedings of the Korean Biophysical Society Conference
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    • 2001.06a
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    • pp.52-52
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    • 2001
  • Nickel-binding protein (NBP1) was purified from the crude extract of Streptomyces seoulensis using Ni$^{2+}$-charged metal chelate affinity chromatography. The molecular mass of NBPI determined on SDS-PAGE was 38kDa. An approximately 3 kb DNA fragment containing the structural gene for NBP1 was cloned from lEMBL3 genomic library of S. seoulensis using a DNA fragment PCR-amplified with the primers designed from N-terminal and internal amino acid sequences of NBP1.(omitted)

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Alternative Polyadenylation of mRNAs: 3'-Untranslated Region Matters in Gene Expression

  • Yeh, Hsin-Sung;Yong, Jeongsik
    • Molecules and Cells
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    • v.39 no.4
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    • pp.281-285
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    • 2016
  • Almost all of eukaryotic mRNAs are subjected to polyadenylation during mRNA processing. Recent discoveries showed that many of these mRNAs contain more than one polyadenylation sites in their 3' untranslated regions (UTR) and that alternative polyadenylation (APA) is prevalent among these genes. Many biological processes such as differentiation, proliferation, and tumorigenesis have been correlated to global APA events in the 3' UTR of mRNAs, suggesting that these APA events are tightly regulated and may play important physiological roles. In this review, recent discoveries in the physiological roles of APA events, as well as the known and proposed mechanisms are summarized. Perspective for future directions is also discussed.

The Dharma of Nonsense-Mediated mRNA Decay in Mammalian Cells

  • Popp, Maximilian Wei-Lin;Maquat, Lynne E.
    • Molecules and Cells
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    • v.37 no.1
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    • pp.1-8
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    • 2014
  • Mammalian-cell messenger RNAs (mRNAs) are generated in the nucleus from precursor RNAs (pre-mRNAs, which often contain one or more introns) that are complexed with an array of incompletely inventoried proteins. During their biogenesis, pre-mRNAs and their derivative mRNAs are subject to extensive cis-modifications. These modifications promote the binding of distinct polypeptides that mediate a diverse array of functions needed for mRNA metabolism, including nuclear export, inspection by the nonsense-mediated mRNA decay (NMD) quality-control machinery, and synthesis of the encoded protein product. Ribonucleoprotein complex (RNP) remodeling through the loss and gain of protein constituents before and after pre-mRNA splicing, during mRNA export, and within the cytoplasm facilitates NMD, ensuring integrity of the transcriptome. Here we review the mRNP rearrangements that culminate in detection and elimination of faulty transcripts by mammalian-cell NMD.