• Title/Summary/Keyword: protein stabilization

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Biophysical effect of lipid modification at palmitoylation site on the structure of Caveolin 3

  • Ma, Yu-Bin;Kang, Dong-Hoon;Kim, Myeongkyu;Kim, Ji-Hun
    • Journal of the Korean Magnetic Resonance Society
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    • v.23 no.3
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    • pp.67-72
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    • 2019
  • Caveolae are small plasma membrane invaginations that play many roles in signal transduction, endocytosis, mechanoprotection, lipid metabolism. The most important protein in caveolae is the integral membrane protein, caveolin, which is divided into three families such as caveolin 1, caveolin 2, and caveolin 3. Caveolin 1 and 3 are known to incorporate palmitate through linkage to three cysteine residues. Regulation of the protein palmitoylation cycle is important for the cellular processes such as intracellular localization of the target protein, membrane association, conformation, protein-protein interaction, and activity. However, the detailed aspect of individual palmitoylation has not been studied. In the present work, the role of each lipid modification at three cysteines was studied by NMR. Our results suggest that each lipid modification at the natively palmitoylation site has its own roles. For example, lipidations to C106 and C129 are play a role in structural stabilization, however, interestingly, lipid modification to C116 interrupts the structural stabilization.

Thermal Stabilization of Aspergillus phytase by L-Arginine

  • Sunghoon Ryu;Park, Tae-Gwan
    • Biotechnology and Bioprocess Engineering:BBE
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    • v.3 no.1
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    • pp.32-34
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    • 1998
  • Phytase from Aspergillus species is a very heat unstable enzyme which inactivates to a great extent during the thermal processing of animal feed formulation. Various protein stabilization additives were tested to improve its heat stability. Among them, a basic amino acid, L-arginine remarkably increased the thermal stability of phytase in an aqueous solution state.

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Stabilization of Lateritic Soil with Eggshell Powder

  • Ndagijima, Jacques;Kim, Kanghyun;Kim, Seunghyun;Shin, Jongho
    • Journal of the Korean GEO-environmental Society
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    • v.23 no.1
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    • pp.5-13
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    • 2022
  • In tropical regions, lateritic soil is frequently used in road embankment. However, it is one of the sources of road failure owing to its low strength. Generally, cement and lime are used as stabilizers for lateritic soil, but they are not environmentally friendly. Some studies try to use eggshells, for they are food waste and share the same chemical composition as lime. Previous researchs have shown that eggshell powder could enhance the strength of lateritic soil. This research investigated the effect of particle size of the eggshell powder and the effect of the protein-membrane presence in the eggshell on stabilizing capacity of soil. Through laboratory tests, unconfined compressive strength was examined for various particle sizes. The particle size of eggshell powder ranging between 150 ㎛ and 88 ㎛ was appropriate size that made an excellent stabilizer at 3% concentration. On the other hand, the protein-membrane reduced the stabilizing ability of the eggshell powder when the content of eggshell powder is less than 4% in soil. Numerical analysis of road embankment was performed based on the results obtained in the laboratory tests. It is shown that the eggshell powder has improved the stability of the sub-base of the road embankment.

Polyamine Prevent Apoptotic Cell Death by Regulation of Apoptosis Related Gene Expression in Porcine Parthenotes

  • Cui, Xiang-Shun;Jin, Yong-Xun;Hwang, Kyu-Chan;Kim, Nam-Hyung
    • Proceedings of the KSAR Conference
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    • 2004.06a
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    • pp.230-230
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    • 2004
  • Polyamines, namely putrescine, spermidine, and spermine, are biogenic low-molecular-weight aliphatic amines. Polyamines play important roles in DNA stabilization, RNA and protein synthesis, membrane stabilization, modulation of ion channels, and protection against oxygen radicals and are essential for cell homeostasis, cell growth, and tumorigenesis. (omitted)

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Molecular analysis of c-terminus structure for elucidating the stabilization effect of site-specific immobilization

  • Baek, Seung-Pil;Yu, Yeong-Jae
    • 한국생물공학회:학술대회논문집
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    • 2001.11a
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    • pp.886-889
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    • 2001
  • C-terminus specific immobilization often results in a increased structural stability resistant to various denaturation factors. In order to elucidate the immobilization effect on the c-terminus in molecular level, we made over 200 protein data set from Protein Data Bank(PDB), analyzed c-terminus structure of each protein, and investigated the structural relationship with the stabilizing factors such as hydrogen bond, ion pairs, cation pi, disulfide bond, solvation free energy, surface area, flexibility and so on.

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Interaction of a 22 kDa Peptidyl Prolyl cis/trans Isomerase with the Heat Shock Protein DnaK in Vibrio anguillarum

  • Kang, Dong Seop;Moon, Soo Young;Cho, Hwa Jin;Lee, Jong Min;Kong, In-Soo
    • Journal of Microbiology and Biotechnology
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    • v.27 no.3
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    • pp.644-647
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    • 2017
  • Peptidyl prolyl cis/trans isomerases (PPIases) catalyze the cis/trans isomerization of peptidyl-prolyl peptide bonds preceding prolines. We investigated the protein-protein interaction between a 22 kDa PPIase (VaFKBP22, an FK506-binding protein) and the molecular chaperone DnaK derived from Vibrio anguillarum O1 (VaDnaK) using GST pull-down assays and a bacterial two-hybrid system for in vivo and in vitro studies, respectively. Furthermore, we analyzed the three-dimensional structure of the protein-protein interaction. Based on our results, VaFKBP22 appears to act as a cochaperone of VaDnaK, and contributes to protein folding and stabilization via its peptidyl-prolyl cis/trans isomerization activity.

DNA Damage-inducible Phosphorylation of p53 at Ser20 is Required for p53 Stabilization

  • Yang, Dong-Hwa;Rhee, Byung-Kirl;Yim, Tae-Hee;Lee, Hye-Jin;Kim, Jungho
    • Animal cells and systems
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    • v.6 no.3
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    • pp.263-269
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    • 2002
  • The p53 tumor suppressor gene is among the most frequently mutated and studied genes in human cancer, but the mechanisms by which it sur presses tumor formation remain unclear. DNA damage regulates both the protein levels of p53 and its affinity for specific DNA sequences. Stabilization of p53 in response to DNA damage is caused by its dissociation from Mdm2, a downstream target gene of p53 and a protein that targets p53 for degradation in the proteosome. Recent studies have suggested that phosphorylation of human p53 at Ser20 is important for stabilizing p53 in response to DNA damage through disruption of the interaction between Mdm2 and p53. We generated mice with an allele encoding changes at Ser20, known to be essential for p53 accumulation following DNA damage, to enable analyses of p53 stabilization in vivo. Our data showed that the mutant p53 was clearly defective for full stabilization of p53 in response to DNA damage. We concluded that Ser20 phosphorylation is critical for modulating the negative regulation of p53 by Mdm2, probably through phosphorylation-dependent inhibition of p53-Mdm2 interaction in the physiological context.

TAGLN2-mediated actin stabilization at the immunological synapse: implication for cytotoxic T cell control of target cells

  • Na, Bo-Ra;Jun, Chang-Duk
    • BMB Reports
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    • v.48 no.7
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    • pp.369-370
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    • 2015
  • Actin dynamics is critical for the formation and sustainment of the immunological synapse (IS) during T cell interaction with antigen-presenting cells (APC). Thus, many actin regulating proteins are involved in spatial and temporal actin remodeling at the IS. However, little is known whether or how actin stabilizing protein controls IS and the consequent T cell functions. TAGLN2 − an actin-binding protein predominantly expressed in T cells − displays a novel function to stabilize cortical F-actin, thereby augmenting F-actin contents at the IS, and acquiring leukocyte function-associated antigen-1 activation following T cell activation. TAGLN2 also competes with cofilin to protect F-actin in vitro and in vivo. During cytotoxic T cell interaction with cancer cells, the expression level of TAGLN2 at the IS correlates with the T cell adhesion to target cancer cells and production of lytic granules such as granzyme B and perforin, thus expressing cytotoxic T cell function. These findings identify a novel function for TAGLN2 as an actin stabilizing protein that is essential for stable immunological synapse formation, thereby regulating T cell immunity. [BMB Reports 2015; 48(7): 369-370]

Stabilization of .betha.-D-galactosidase from heat and chemical inactivation with the extract of panax ginseng C. A. Meyer

  • Kim, Doo-Ha;Hahn, Younghe;Hong, Soon-Keun
    • Archives of Pharmacal Research
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    • v.5 no.2
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    • pp.45-52
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    • 1982
  • Staibilization effect of Panax ginseng C. A. Meyer on .betha.-D-Galactosidase inactivation was proved by kinetic studies of thermal inactivation of the enzyme. The water extract Panax ginseng C. A. Meyer showed stabilization activity at minimal concentration of 10ppm. The methanolic extract was purified to obtain ginseng saponins, and two groups of the ginsenosides, i. e. protopanaxadiol and protopanaxatriol were isolated. They also showed a protective effect against the thermal and chemical inactivation of the enzyme; p-chloromercuribenzoic acid and hydroxylamine known as protein modifier greatly inactivated the enzyme but inactivation was significantly balocked by the ginseng component MG$^{2+}$, known as a cofactor, stabilized the enzyme and the poor stabilization effect by it was potentiated by ginseng components.s.

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