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Bioluminescent detection of tick-borne encephalitis virus in native ticks / A. N. Kudryavtsev, L. P. Burakova, L. A. Frank // Anal. Methods. - 2017. - Vol. 9, Is. 15. - P2252-2255, DOI 10.1039/c7ay00535k . - ISSN 1759-9660
Кл.слова (ненормированные):
Proteins -- Recombinant proteins -- Viruses -- Binding proteins -- Bioluminescence
Аннотация: A one-step bioluminescent immunoassay for tick-borne encephalitis virus (TBEV) in natural ticks based on the hybrid protein 14D5a-Rm7 was developed. Recombinant Ca2+-dependent coelenterazine-binding protein was shown to be a more convenient substrate form for the Rm7 domain than coelenterazine. Over 600 samples of natural ticks were analyzed and shown to have essential differences in the discrimination factor D for TBEV-positive (2.77 ± 0.81) and TBEV-negative (1.15 ± 0.28) samples. © The Royal Society of Chemistry.

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Держатели документа:
Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, Russian Federation
Siberian Federal University, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Kudryavtsev, A. N.; Burakova, L. P.; Frank, L. A.

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Unanimous Model for Describing the Fast Bioluminescence Kinetics of Ca2+-regulated Photoproteins of Different Organisms / E. V. Eremeeva [et al.] // Photochem. Photobiol. - 2017. - Vol. 93, Is. 2. - P495-502, DOI 10.1111/php.12664. - Cited References:55. - This work was supported by RFBR grant 14-04-31092 and the state budget allocated to the fundamental research at the Russian Academy of Sciences (projects 01201351504 and 01201351502). . - ISSN 0031-8655. - ISSN 1751-1097

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
GREEN-FLUORESCENT PROTEIN
AEQUORIN BIOLUMINESCENCE
SEQUENCE-ANALYSIS
Аннотация: Upon binding their metal ion cofactors, Ca2+-regulated photoproteins display a rapid increase of light signal, which reaches its peak within milliseconds. In the present study, we investigate bioluminescence kinetics of the entire photoprotein family. All five recombinant hydromedusan Ca2+-regulated photoproteinsaequorin from Aequorea victoria, clytin from Clytia gregaria, mitrocomin from Mitrocoma cellularia and obelins from Obelia longissima and Obelia geniculatademonstrate the same bioluminescent kinetics pattern. Based on these findings, for the first time we propose a unanimous kinetic model describing the bioluminescence mechanism of Ca2+-regulated photoproteins.

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Держатели документа:
Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Fed Res Ctr, Photobiol Lab, Krasnoyarsk, Russia.
Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Fed Res Ctr, Theoret Biophys Lab, Krasnoyarsk, Russia.
Wageningen Univ & Res, Biochem Lab, Wageningen, Netherlands.

Доп.точки доступа:
Eremeeva, Elena V.; Bartsev, Sergey I.; van Berkel, Willem J. H.; Vysotski, Eugene S.; RFBR [14-04-31092]; Russian Academy of Sciences [01201351504, 01201351502]

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Tyr72 and Tyr80 are Involved in the Formation of an Active Site of a Luciferase of Copepod Metridia longa / M. D. Larionova, S. V. Markova, E. S. Vysotski // Photochem. Photobiol. - 2017. - Vol. 93, Is. 2. - P503-510, DOI 10.1111/php.12694. - Cited References:41. - This work was supported by the grant 14-14-01119 of the Russian Science Foundation. . - ISSN 0031-8655. - ISSN 1751-1097

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
CA2+-REGULATED PHOTOPROTEIN OBELIN
COELENTERAZINE-BINDING PROTEIN
Аннотация: Luciferase of copepod Metridia longa (MLuc) is a naturally secreted enzyme catalyzing the oxidative decarboxylation of coelenterazine with the emission of light. To date, three nonallelic isoforms of different lengths (17-24 kDa) for M. longa luciferase have been cloned. All the isoforms are single-chain proteins consisting of a 17-residue signal peptide for secretion, variable N-terminal part and conservative C-terminus responsible for luciferase activity. In contrast to other bioluminescent proteins containing a lot of aromatic residues which are frequently involved in light emission reaction, the C-terminal part of MLuc contains only four Phe, two Tyr, one Trp and two His residues. To figure out whether Tyr residues influence bioluminescence, we constructed the mutants with substitution of Tyr to Phe (Y72F and Y80F). Tyrosine substitutions do not eliminate the ability of luciferase to bioluminescence albeit significantly reduce relative specific activity and change bioluminescence kinetics. In addition, the Tyr replacements have no effect on bioluminescence spectrum, thereby indicating that tyrosines are not involved in the emitter formation. However, as it was found that the intrinsic fluorescence caused by Tyr residues is quenched by a reaction substrate, coelenterazine, in concentration-dependent manner, we infer that both tyrosine residues are located in the luciferase substrate-binding cavity.

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Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Fed Res Ctr, Photobiol Lab, Krasnoyarsk, Russia.
Siberian Fed Univ, Chair Biophys, Krasnoyarsk, Russia.

Доп.точки доступа:
Larionova, Marina D.; Markova, Svetlana V.; Vysotski, Eugene S.; Russian Science Foundation [14-14-01119]

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Fluorescent coelenteramide-containing protein as a color bioindicator for low-dose radiation effects / A. S. Petrova [et al.] // Anal. Bioanal. Chem. - 2017. - Vol. 409, Is. 18. - P4377-4381, DOI 10.1007/s00216-017-0404-9. - Cited References:22. - This work was supported by the state budget allocated to the fundamental research at the Russian Academy of Sciences (project 01201351504) and by the Russian Foundation for Basic Research, Grant No. 16-34-00695. . - ISSN 1618-2642. - ISSN 1618-2650

РУБ Biochemical Research Methods + Chemistry, Analytical
Рубрики:
LUMINOUS MARINE-BACTERIA
DISCHARGED-OBELIN
AEQUORIN
Кл.слова (ненормированные):
Fluorescent protein -- Coelenteramide -- Discharged photoprotein obelin -- Multicolor bioindicator -- Radiotoxicity
Аннотация: The study addresses the application of fluorescent coelenteramide-containing proteins as color bioindicators for radiotoxicity evaluation. Biological effects of chronic low-dose radiation are under investigation. Tritiated water (200 MBq/L) was used as a model source of low-intensive ionizing radiation of beta type. 'Discharged obelin,' product of bioluminescent reaction of marine coelenterate Obelia longissimi, was used as a representative of the coelenteramide-containing proteins. Coelenteramide, fluorophore of discharged obelin, is a photochemically active molecule; it produces fluorescence forms of different color. Contributions of 'violet' and 'blue-green' forms to the visible fluorescence serve as tested parameters. The contributions depend on the coelenteramide's microenvironment in the protein, and, hence, evaluate distractive ability and toxicity of radiation. The protein samples were exposed to beta radiation for 18 days, and maximal dose accumulated by the samples was 0.28 Gy, being close to a tentative limit of a low-dose interval. Increase of relative contribution of 'violet' fluorescence under exposure to the beta irradiation was revealed. High sensitivity of the protein-based test system to low-dose ionizing radiation (to 0.03 Gy) was demonstrated. The study develops physicochemical understanding of radiotoxic effects.

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Держатели документа:
FRC KSC SB RAS, Inst Biophys SB RAS, Akademgorodok 50, Krasnoyarsk 660036, Russia.
Krasnoyarsk State Agrarian Univ, Krasnoyarsk 660049, Russia.
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
Moscow MV Lomonosov State Univ, Moscow 119991, Russia.

Доп.точки доступа:
Petrova, Alena S.; Lukonina, Anna A.; Badun, Gennadii A.; Kudryasheva, Nadezhda S.; Russian Academy of Sciences [01201351504]; Russian Foundation for Basic Research [16-34-00695]

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Inhibition effect of food preservatives on endoproteinases / E. N. Esimbekova [et al.] // Food Chem. - 2017. - Vol. 235. - P294-297, DOI 10.1016/j.foodchem.2017.05.059 . - ISSN 0308-8146
Кл.слова (ненормированные):
Endoproteinases -- Food additives -- Pancreatic disease -- Pancreatic enzymes -- Benzoic acid -- Enzyme activity -- Enzymes -- Food additives -- Food preservatives -- Potassium sorbate -- Sodium -- Acceptable daily intakes -- Decay constants -- Endoproteinases -- Human metabolisms -- Inhibition effect -- Light intensity -- Protein digestion -- Sodium benzoate -- Sorbic acid
Аннотация: The present manuscript proposes a novel approach to assess the impact of food additives on human metabolism by analysing their effect on biomarker enzyme activity. Alterations in the activity of pancreatic enzymes, such as chymotrypsin and trypsin, which are affected by the most common food preservatives, sodium benzoate (E211), potassium sorbate (E202) and sorbic acid (E200), have been evaluated. The proteinase activity was analysed with a bioluminescent method using the light intensity decay constant. Our study revealed that the preservatives reduce proteinase activity by 50% (EC50) at a much lower concentration than their acceptable daily intake (ADI). Thus, sodium benzoate and sorbic acid have an inhibition effect on chymotrypsin at concentrations 14 times lower and 70 times lower than their ADI and this increases with exposure time. Food preservative consumption impacts negatively on protein digestion, which is especially dangerous for patients with pancreatitis. © 2017 Elsevier Ltd

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Держатели документа:
Institute of Biophysics SB RAS, Federal Research Center ‘Krasnoyarsk Science Center SB RAS’, Krasnoyarsk, Russian Federation
Siberian Federal University, Institute of Fundamental Biology and Biotechnology, Krasnoyarsk, Russian Federation
Krasnoyarsk State Agricultural University, Institute of Agro-ecological Technologies, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Esimbekova, E. N.; Asanova, A. A.; Deeva, A. A.; Kratasyuk, V. A.

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Variability of fluorescence spectra of coelenteramide-containing proteins as a basis for toxicity monitoring / R. R. Alieva, N. S. Kudryasheva // Talanta. - 2017. - Vol. 170. - P425-431, DOI 10.1016/j.talanta.2017.04.043 . - ISSN 0039-9140
Кл.слова (ненормированные):
Coelenteramide-containing fluorescent protein -- Multicolor fluorescent bioassay -- Obelin -- Primary photochemical process -- Protein destruction -- Proton transfer -- Bioassay -- Biomarkers -- Excited states -- Fluorescence -- Fluorophores -- Ionizing radiation -- Proton transfer -- Toxicity -- Electron-excited state -- Fluorescence spectra -- Fluorescent protein -- Green fluorescent protein -- Obelin -- Photochemical process -- Photochemical properties -- Physicochemical process -- Proteins
Аннотация: Nowadays, physicochemical approach to understanding toxic effects remains underdeveloped. A proper development of such mode would be concerned with simplest bioassay systems. Coelenteramide-Containing Fluorescent Proteins (CLM-CFPs) can serve as proper tools for study primary physicochemical processes in organisms under external exposures. CLM-CFPs are products of bioluminescent reactions of marine coelenterates. As opposed to Green Fluorescent Proteins, the CLM-CFPs are not widely applied in biomedical research, and their potential as colored biomarkers is undervalued now. Coelenteramide, fluorophore of CLM-CFPs, is a photochemically active molecule; it acts as a proton donor in its electron-excited states, generating several forms of different fluorescent state energy and, hence, different fluorescence color, from violet to green. Contributions of the forms to the visible fluorescence depend on the coelenteramide microenvironment in proteins. Hence, CLM-CFPs can serve as fluorescence biomarkers with color differentiation to monitor results of destructive biomolecule exposures. The paper reviews experimental and theoretical studies of spectral-luminescent and photochemical properties of CLM-CFPs, as well as their variation under different exposures – chemicals, temperature, and ionizing radiation. Application of CLM-CFPs as toxicity bioassays of a new type is justified. © 2017

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Держатели документа:
Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Akademgorodok 50/50, Krasnoyarsk, Russian Federation
Siberian Federal University, Svobodny Prospect 79, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Alieva, R. R.; Kudryasheva, N. S.

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Hybrid Minimal Core Streptavidin–Obelin as a Versatile Reporter for Bioluminescence-based Bioassay / E. E. Bashmakova [et al.] // Photochem. Photobiol. - 2017. - Vol. 93, Is. 2. - P548-552, DOI 10.1111/php.12648 . - ISSN 0031-8655
Аннотация: Ca2+-regulated photoprotein obelin was genetically fused with a minimum-sized core streptavidin. Hybrid protein (SAV–OL) was produced by bacterial expression and applied as a specific bioluminescent probe in diverse solid-phase assays. The obtained results clearly demonstrate specific activity of each domain indicating its proper folding with favorable space orientation. SAV–OL has been shown to be a much more sensitive label than the chemical conjugate of a full-length streptavidin with obelin. © 2016 The American Society of Photobiology

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Держатели документа:
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Krasnoyarsk, Russian Federation
Siberian Federal University, Krasnoyarsk, Russian Federation
Chemistry Department, Lomonosov Moscow State University, Moscow, Russian Federation

Доп.точки доступа:
Bashmakova, E. E.; Krasitskaya, V. V.; Kudryavtsev, A. N.; Grigorenko, V. G.; Frank, L. A.

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Ultraviolet fluorescence of coelenteramide and coelenteramide-containing fluorescent proteins. Experimental and theoretical study / R. R. Alieva [et al.] // J. Photochem. Photobiol. B Biol. - 2016. - Vol. 162. - P318-323, DOI 10.1016/j.jphotobiol.2016.07.004 . - ISSN 1011-1344
Кл.слова (ненормированные):
Aequorin -- B3LYP -- Coelenteramide -- Discharged photoproteins -- Excitation energy -- Fluorescence -- Fluorescent protein -- Obelin
Аннотация: Coelenteramide-containing fluorescent proteins are products of bioluminescent reactions of marine coelenterates. They are called ‘discharged photoproteins’. Their light-induced fluorescence spectra are variable, depending considerably on external conditions. Current work studies a dependence of light-induced fluorescence spectra of discharged photoproteins obelin, aequorin, and clytin on excitation energy. It was demonstrated that photoexcitation to the upper electron-excited states (260–300 nm) of the discharged photoproteins initiates a fluorescence peak in the near UV region, in addition to the blue-green emission. To characterize the UV fluorescence, the light-induced fluorescence spectra of coelenteramide (CLM), fluorophore of the discharged photoproteins, were studied in methanol solution. Similar to photoproteins, the CLM spectra depended on photoexcitation energy; the additional peak (330 nm) in the near UV region was observed in CLM fluorescence at higher excitation energy (260–300 nm). Quantum chemical calculations by time depending method with B3LYP/cc-pVDZ showed that the conjugated pyrazine-phenolic fragment and benzene moiety of CLM molecule are responsible for the additional UV fluorescence peak. Quantum yields of CLM fluorescence in methanol were 0.028 ± 0.005 at 270–340 nm photoexcitation. A conclusion was made that the UV emission of CLM might contribute to the UV fluorescence of the discharged photoproteins. The study develops knowledge on internal energy transfer in biological structures – complexes of proteins with low-weight aromatic molecules. © 2016 Elsevier B.V.

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Держатели документа:
Institute of Biophysics SB RAS, Akademgorodok 50/50, Krasnoyarsk, Russian Federation
Institute of Physics SB RAS, Akademgorodok 50/38, Krasnoyarsk, Russian Federation
Siberian Federal University, Svobodny Prospect 79, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Alieva, R. R.; Tomilin, F. N.; Kuzubov, A. A.; Ovchinnikov, S. G.; Kudryasheva, N. S.

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Similarity of decay-associated spectra for tryptophan fluorescence of proteins with different structures / E. V. Nemtseva, O. O. Lashchuk, M. A. Gerasimova // Biophysics. - 2016. - Vol. 61, Is. 2. - P193-199, DOI 10.1134/S0006350916020111 . - ISSN 0006-3509
Кл.слова (ненормированные):
denaturation -- dielectric relaxation -- fluorescence lifetime -- tertiary protein structure -- tryptophan
Аннотация: Tryptophan fluorescence lifetimes were analyzed for three proteins: human serum albumin, bovine serum albumin, and bacterial luciferase, which contain one, two, and seven tryptophan residues, respectively. For all of the proteins, the fluorescence decays were fitted by three lifetimes: ?1 = 6–7 ns, ?2 = 2.0–2.3 ns, and ?3 ? 0.1 ns (the native state), and ?1 = 4.4–4.6 ns, ?2 = 1.7–1.8 ns, and ?3 ? 0.1 ns (the denatured state). Corresponding decay-associated spectra had similar peak wavelengths and spectrum half-widths both in the native state (??1max = 342 nm, ??2max = 328 nm, and ??3max = 315 nm), and in the denatured state (??1max = 350 nm, ??2max= 343 nm, and ??3max= 317 nm). The differences in the steady-state spectra of the studied proteins were accounted for the individual ratio of the lifetime component contributions. The lifetime components were compared with a classification of tryptophan residues in the structure of these proteins within the discrete states model. © 2016, Pleiades Publishing, Inc.

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Держатели документа:
Siberian Federal University, Svobodnyi pr. 79, Krasnoyarsk, Russian Federation
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Akademgorodok 50/50, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Nemtseva, E. V.; Lashchuk, O. O.; Gerasimova, M. A.

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10.

Spectral Changes of Erythrosin B Luminescence Upon Binding to Bovine Serum Albumin [Text] / N. V. Sablin, M. A. Gerasimova, E. V. Nemtseva // Russ. Phys. J. - 2016. - Vol. 58, Is. 12. - P1797-1803, DOI 10.1007/s11182-016-0719-6. - Cited References:16. - This work was supported in part by the Russian Academy of Sciences (The program "Molecular and Cell Biology", project No. 6.8), the Ministry of Education and Science of the Russian Federation (project No. 1762), and the Federal Agency of scientific organizations of the Russian Federation (project No. VI 57.1.1). . - ISSN 1064-8887. - ISSN 1573-9228

РУБ Physics, Multidisciplinary
Рубрики:
ROOM-TEMPERATURE
   AQUEOUS-SOLUTION
   PHOSPHORESCENCE
   FLUORESCENCE
   EOSIN
Кл.слова (ненормированные):
erythrosin B -- phosphorescence -- delayed fluorescence -- quantum yield -- phosphorescence lifetime -- bovine serum albumin
Аннотация: Changes in absorption, fluorescence, phosphorescence, and delayed fluorescence spectra of erythrosin B are studied in the presence of bovine serum albumin at room temperature. Spectral and chronoscopic characteristics of the observed photophysical processes are defined. The binding of erythrosin B with the protein followed by spectral changes is demonstrated. Absorption and fluorescence spectra of the dye in the bound state are described, the binding mechanism is analyzed. The binding parameters of the dye-protein complex are estimated.

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Держатели документа:
Siberian Fed Univ, Krasnoyarsk, Russia.
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk, Russia.

Доп.точки доступа:
Sablin, N. V.; Gerasimova, M. A.; Nemtseva, E. V.; Russian Academy of Sciences [6.8]; Ministry of Education and Science of the Russian Federation [1762]; Federal Agency of scientific organizations of the Russian Federation [VI 57.1.1]

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11.

The novel extremely psychrophilic luciferase from Metridia longa: Properties of a high-purity protein produced in insect cells / M. D. Larionova, S. V. Markova, E. S. Vysotski // Biochem. Biophys. Res. Commun. - 2017. - Vol. 483, Is. 1. - P772-778, DOI 10.1016/j.bbrc.2016.12.067. - Cited References:24. - The cloning of cDNAs encoding MLuc2 isoforms of M. longa was supported by Bayer AG (Germany) and the state budget allocated to the fundamental research at the Russian Academy of Sciences (project No. 01201351504); all other studies were funded by RFBR and Government of Krasnoyarsk Territory according to the research project No. 16-44-242099. . - ISSN 0006-291X. - ISSN 1090-2104

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
CDNA CLONING
EXPRESSION
ENZYME
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Bioluminescent reporter -- Psychrophilic -- enzyme -- Molecular adaptation
Аннотация: The bright bioluminescence of copepod Metridia longa is conditioned by a small secreted coelenterazinedependent luciferase (MLuc). To date, three isoforms of MLuc differing in length, sequences, and some properties were cloned and successfully applied as high sensitive bioluminescent reporters. In this work, we report cloning of a novel group of genes from M. longa encoding extremely psychrophilic isoforms of MLuc (MLuc2-type). The novel isoforms share only similar to 54-64% of protein sequence identity with the previously cloned isoforms and, consequently, are the product of a separate group of paralogous genes. The MLuc2 isoform with consensus sequence was produced as a natively folded protein using baculovirus/ insect cell expression system, purified, and characterized. The MLuc2 displays a very high bioluminescent activity and high thermostability similar to those of the previously characterized M. longa luciferase isoform MLuc7. However, in contrast to MLuc7 revealing the highest activity at 12-17 degrees C and 0.5 M NaCl, the bioluminescence optima of MLuc2 isoforms are at similar to 5 degrees C and 1 M NaCl. The MLuc(2) adaptation to cold is also accompanied by decrease of melting temperature and affinity to substrate suggesting a more conformational flexibility of a protein structure. The luciferase isoforms with different temperature optima may provide adaptability of the M. longa bioluminescence to the changes of water temperature during diurnal vertical migrations. (C) 2016 Elsevier Inc. All rights reserved.

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Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Inst Biophys SB RAS, Photobiol Lab, Krasnoyarsk, Russia.
Siberian Fed Univ, Krasnoyarsk, Russia.

Доп.точки доступа:
Larionova, Marina D.; Markova, Svetlana V.; Vysotski, Eugene S.; Bayer AG (Germany); Russian Academy of Sciences [01201351504]; RFBR; Government of Krasnoyarsk Territory [16-44-242099]

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12.

Variation of Spectral Characteristics of Coelenteramide-Containing Fluorescent Protein from Obelia Longissima Exposed to Dimethyl Sulfoxide / A. S. Petrova [et al.] // Russ. Phys. J. - 2016. - Vol. 59, Is. 4. - P562-567, DOI 10.1007/s11182-016-0806-8. - Cited References:33. - This work was supported in part by the Russian Science Foundation (Contract No. 14-14-00076). . - ISSN 1064-8887. - ISSN 1573-9228

РУБ Physics, Multidisciplinary
Рубрики:
CA2+-REGULATED PHOTOPROTEINS
SPECTROSCOPIC PROPERTIES
Кл.слова (ненормированные):
fluorescent coelenteramide-containing fluorescent proteins -- discharged -- obelin -- proton transfer -- dimethyl sulfoxide
Аннотация: Effect of dimethyl sulfoxide (DMSO), a widespread biomedical agent, on spectral-luminescent characteristics of coelenteramide-containing fluorescent protein - discharged obelin - is investigated. Contributions of violet and blue-green spectral components to fluorescence of discharged obelin are elucidated and characterized at different photoexcitation energies. Dependences of these contributions on the DMSO concentration are presented. Spectral changes are related to the destructive effect of DMSO on fluorescent protein and decreasing efficiency of proton transfer to electronically excited states of fluorophore.

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Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk, Russia.
Siberian Fed Univ, Krasnoyarsk, Russia.
Krasnoyarsk State Agrarian Univ, Krasnoyarsk, Russia.

Доп.точки доступа:
Petrova, A. S.; Alieva, R. R.; Belogurova, N. V.; Tirranen, L. S.; Kudryasheva, N. S.; Russian Science Foundation [14-14-00076]

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13.

Experimental wound dressings of degradable PHA for skin defect repair / E. I. Shishatskaya [et al.] // J. Mater. Sci. Mater. Med. - 2016. - Vol. 27, Is. 11, DOI 10.1007/s10856-016-5776-4 . - ISSN 0957-4530
Кл.слова (ненормированные):
Biomaterials -- Cell culture -- Cells -- Cytology -- Enzyme inhibition -- Fibroblasts -- Membranes -- Natural polymers -- Nonwoven fabrics -- Polymer films -- Proteins -- Stem cells -- Weaving -- Electrospun membranes -- Extracellular matrix protein -- Fibroblast cells -- Hydroxyderivative -- Mesenchymal stem cell -- Non-woven membranes -- Wound dressing materials -- Wound healing process -- Tissue
Аннотация: The present study reports construction of wound dressing materials from degradable natural polymers such as hydroxy derivatives of carboxylic acids (PHAs) and 3-hydroxybutyrate/4-hydroxybutyrate [P(3HB/4HB)] as copolymer. The developed polymer films and electrospun membranes were evaluated for its wound healing properties with Grafts—elastic nonwoven membranes carrying fibroblast cells derived from adipose tissue multipotent mesenchymal stem cells. The efficacy of nonwoven membranes of P(3HB/4HB) carrying the culture of allogenic fibroblasts was assessed against model skin defects in Wistar rats. The morphological, histological and molecular studies revealed the presence of fibroblasts on dressing materials which facilitated wound healing, vascularization and regeneration. Further it was also observed that cells secreted extracellular matrix proteins which formed a layer on the surface of membranes and promoted the migration of epidermal cells from the neighboring tissues surrounding the wound. The wounds under the P(3HB/4HB) membrane carrying cells healed 1.4 times faster than the wounds under the cell-free membrane and 3.5 times faster than the wounds healing under the eschar (control).The complete wound healing process was achieved at Day 14. Thus the study highlights the importance of nonwoven membranes developed from degradable P(3HB/4HB) polymers in reducing inflammation, enhancing angiogenic properties of skin and facilitating better wound healing process. © 2016, Springer Science+Business Media New York.

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Держатели документа:
Institute of Biophysics of Siberian Branch of Russian Academy of Sciences, 50-50 Akademgorodok, Krasnoyarsk, Russian Federation
Siberian Federal University, 79 Svobodniy Ave., Krasnoyarsk, Russian Federation

Доп.точки доступа:
Shishatskaya, E. I.; Nikolaeva, E. D.; Vinogradova, O. N.; Volova, T. G.

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14.

Effect of viscosity on efficiency of enzyme catalysis of bacterial luciferase coupled with lactate dehydrogenase and NAD(P)H:FMN-Oxidoreductase / O. S. Sutormin [et al.] // Mol. Cat. - 2018. - Vol. 458. - P60-66, DOI 10.1016/j.mcat.2018.08.012 . - ISSN 2468-8231
Кл.слова (ненормированные):
Bioluminescence -- Coupling of enzymes -- In vivo simulated media -- Metabolic chain -- Protein stability
Аннотация: One of the current trends of the modern biology figures out cellular enzyme behaviour. Numerous researches look more closely at the chemical composition of creating in vivo simulated media conditions. The aim of this work was to find out a thermodynamic cooperativity of enzymes in a triple-enzyme chain (lactate dehydrogenase + NAD(P)H: FMN-oxidoreductase + bacterial luciferase) under in vivo simulated condition. The thermodynamic cooperativity effects were found out based on the influence of the viscogens (glycerol and sucrose) on the thermal stability of the triple-enzyme system. The results showed that the viscogens do not lead to an increase in the thermal stability of the triple-enzyme system. In addition, organic solvents (sucrose and glycerol) added as viscous agents to the reaction medium altered the kinetics of this triple-enzyme chain, including changing the light emission decay constant (kdec) and quantum yield of luminescence (Q). Plus, sucrose was found to be more efficient in limiting the flexibility of enzymes than glycerol. The high sensitivity of the triple-enzyme system to the viscogens may be connected with a fact that lactate dehydrogenase does not bound with couple enzyme system NAD(P)H: FMN-oxidoreductase + bacterial luciferase inside the real cell. Since this approach may be used as a method to understand the real connection between enzymes in cellular multi-enzyme metabolic chains inside the luminous bacteria cell. © 2018 Elsevier B.V.

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Держатели документа:
Department of Biophysics, Institute of Fundamental Biology and Biotechnology, Siberian Federal University, Krasnoyarsk, Russian Federation
Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Federal Research Center ‘Krasnoyarsk Science Center SB RAS’, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Sutormin, O. S.; Sukovataya, I. E.; Pande, S.; Kratasyuk, V. A.

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15.

Protein-based fluorescent bioassay for low-dose gamma radiation exposures / A. S. Petrova [et al.] // Anal. Bioanal. Chem. - 2018, DOI 10.1007/s00216-018-1282-5 . - ISSN 1618-2642
Кл.слова (ненормированные):
Bioassay -- Enzymes -- Fluorescence/luminescence -- Fluorescent protein -- Gamma radiation -- Radiotoxicity -- Efficiency -- Enzymes -- Fluorescence -- Gamma rays -- Proteins -- Proton transfer -- Fluorescence characteristics -- Fluorescence intensities -- Fluorescence spectra -- Fluorescence/luminescence -- Fluorescent protein -- Photochemical process -- Physiological liquids -- Radiotoxicity -- Bioassay
Аннотация: The study suggests an application of a coelenteramide-containing fluorescent protein (CLM-CFP) as a simplest bioassay for gamma radiation exposures. “Discharged obelin,” a product of the bioluminescence reaction of the marine coelenterate Obelia longissima, was used as a representative of the CLM-CFP group. The bioassay is based on a simple enzymatic reaction—photochemical proton transfer in the coelenteramide-apoprotein complex. Components of this reaction differ in fluorescence color, providing, by this, an evaluation of the proton transfer efficiency in the photochemical process. This efficiency depends on the microenvironment of the coelenteramide within the protein complex, and, hence, can evaluate a destructive ability of gamma radiation. The CLM-CFP samples were exposed to gamma radiation (137Cs, 2 mGy/h) for 7 and 16 days at 20 °C and 5 °C, respectively. As a result, two fluorescence characteristics (overall fluorescence intensity and contributions of color components to the fluorescence spectra) were identified as bioassay parameters. Both parameters demonstrated high sensitivity of the CLM-CFP-based bioassay to the low-dose gamma radiation exposure (up to 100 mGy). Higher temperature (20 °C) enhanced the response of CLM-CFP to gamma radiation. This new bioassay can provide fluorescent multicolor assessment of protein destruction in cells and physiological liquids under exposure to low doses of gamma radiation. [Figure not available: see fulltext.]. © 2018, Springer-Verlag GmbH Germany, part of Springer Nature.

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Держатели документа:
Krasnoyarsk State Agrarian University, Mira Avenue 90, Krasnoyarsk, Russian Federation
Siberian Federal University, Svobodnyy Ave 79, Krasnoyarsk, Russian Federation
Institute of Biophysics SB RAS, FRC KSC SB RAS, Krasnoyarsk, Russian Federation
Department of Radiology, University of Pennsylvania, 3401 N Broad St., Philadelphia, PA, United States

Доп.точки доступа:
Petrova, A. S.; Lukonina, A. A.; Dementyev, D. V.; Bolsunovsky, A. Ya. ; Popov, A. V.; Kudryasheva, N. S.

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16.

Novel 2 '-F-RNA aptamers specific to protein markers of glycemia - a basis for bioluminescent aptasensors / M. Vorobyeva [et al.] // FEBS Open Bio. - 2018. - Vol. 8. - P118-118. - Cited References:0. - The work is supported by Russian Science Foundation (Grant No. 16-14-10296). . - ISSN 2211-5463

РУБ Biochemistry & Molecular Biology

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Держатели документа:
RAS, SB, Inst Chem Biol & Fundamental Med, Novosibirsk, Russia.
Novosibirsk State Univ, Novosibirsk, Russia.
RAS, Inst Biophys, SB, Fed Res Ctr,Krasnoyarsk Sci Ctr, Krasnoyarsk, Russia.
Siberian Fed Univ, Krasnoyarsk, Russia.
Доп.точки доступа:
Vorobyeva, M.; Davydova, A.; Shatunova, E.; Vorobjev, P.; Tupikin, A.; Kabilov, M.; Bashmakova, E.; Krasitskaya, V.; Frank, L.; Venyaminova, A.; Russian Science Foundation [16-14-10296]

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17.

Experimental approach to study the effect of mutations on the protein folding pathway / E. V. Nemtseva [et al.] // PLoS One. - 2019. - Vol. 14, Is. 1. - Ст. e0210361, DOI 10.1371/journal.pone.0210361. - Cited References:38. - The study of time-resolved protein fluorescence was supported by the Ministry of Science and Education of the Russian Federation (Projects 6.7734.2017). The investigation of protein fluorescence and genetic engineering studies of bovine carbonic anhydrase II were supported by grant N14-24-00157 from the Russian Science Foundation. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.; The study of time-resolved protein fluorescence was supported by the Ministry of Science and Education of the Russian Federation (Project 6.7734.2017). The investigation of protein fluorescence and genetic engineering studies of bovine carbonic anhydrase II were supported by grant N14-24-00157 from the Russian Science Foundation. . - ISSN 1932-6203

РУБ Multidisciplinary Sciences
Рубрики:
FLUORESCENCE LIFETIMES ORIGIN
   TRANSITION-STATE
   EXCHANGE
   TRYPTOPHAN
Аннотация: Is it possible to compare the physicochemical properties of a wild-type protein and its mutant form under the same conditions? Provided the mutation has destabilized the protein, it may be more correct to compare the mutant protein under native conditions to the wild-type protein destabilized with a small amount of the denaturant. In general, is it appropriate to compare the properties of proteins destabilized by different treatments: mutations, pH, temperature, and denaturants like urea? These issues have compelled us to search for methods and ways of presentation of experimental results that would allow a comparison of mutant forms of proteins under different conditions and lead to conclusions on the effect of mutations on the protein folding/unfolding pathway. We have studied equilibrium unfolding of wild-type bovine carbonic anhydrase II (BCA II) and its six mutant forms using different urea concentrations. BCA II has been already studied in detail and is a good model object for validating new techniques. In this case, time-resolved fluorescence spectroscopy was chosen as the basic research method. The main features of this experimental method allowed us to compare different stages of unfolding of studied proteins and prove experimentally that a single substitution of the amino acid in three mutant forms of BCA II affected the native state of the protein but did not change its unfolding pathway. On the contrary, the inserted disulfide bridge in three other mutant forms of BCA II affected the protein unfolding pathway. An important result of this research is that we have validated the new approach allowing investigation of the effect of mutations on the folding of globular proteins, because in this way it is possible to compare proteins in the same structural states rather than under identical conditions.

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Держатели документа:
Siberian Fed Univ, Krasnoyarsk, Russia.
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk, Russia.
Russian Acad Sci, Inst Prot Res, Pushchino, Moscow Region, Russia.

Доп.точки доступа:
Nemtseva, Elena V.; Gerasimova, Marina A.; Melnik, Tatiana N.; Melnik, Bogdan S.; Gerasimova, Marina; Nemtseva, Elena; Ministry of Science and Education of the Russian Federation [6.7734.2017]; Russian Science Foundation [N14-24-00157]

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18.

Is Body Mass Index a potential biomarker for anemia in obese adolescents? / S. Pande, R. Ranjan, V. A. Kratasyuk // J. Nutr. Intermediary Metab. - 2019. - Vol. 15. - P1-2, DOI 10.1016/j.jnim.2018.11.001 . - ISSN 2352-3859
Кл.слова (ненормированные):
Anemia -- Body Mass Index -- Hepcidin -- Leptin -- Obesity
Аннотация: The two paradoxical major health problems namely obesity and anemia are confirmed to affect millions around the world. Hepcidin, a protein synthesized in liver is a negative iron binding regulator. There is an affirmative relation between hepcidin and leptin levels and an inverse co-relation between hepcidin and iron status due to inflammation mediated by obesity in adolescents. So this implicates an alliance between anemia and obesity wherein weight reduction can be a powerful medium to improve iron absorption in obese adolescents. Also the Body Mass Index can serve as a preliminary non-invasive screening tool to identify potential adolescents prone to anemia. © 2018

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Laboratory of Bioluminescent Biotechnologies, Department of Biophysics, Institute of Fundamental Biology and Biotechnology, Siberian Federal University, 79 Svobodny Prospect, Krasnoyarsk, 660041, Russian Federation
Institute of Biophysics SB RAS, Federal Research Center ‘Krasnoyarsk Science Center SB RAS’, Akademgorodok 50/50, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Pande, S.; Ranjan, R.; Kratasyuk, V. A.

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19.

Nonspecific stress response to temperature increase in Gammarus lacustris Sars with respect to oxygen-limited thermal tolerance concept / K. Vereshchagina [et al.] // PeerJ. - 2018. - Vol. 6. - Ст. e5571, DOI 10.7717/peerj.5571. - Cited References:49. - The study was carried out with the main financial support of Russian Science Foundation grant 17-14-01063, with the partial financial support of Russian Foundation for Basic Research grants 16-34-00687, 16-34-60060, 17-34-50012, the base part of Goszadanie project 6.9654.2017/8.9, joint program of DAAD and Ministry of education and Science M. Lomonosov (6.12735.2018/12.2) and Lake Baikal Foundation (FOB_02-3/05). There was no additional external funding received for this study. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. . - ISSN 2167-8359

РУБ Multidisciplinary Sciences
Рубрики:
COPEPOD TIGRIOPUS-JAPONICUS
SHUNET SOUTH SIBERIA
HEAT-SHOCK PROTEINS
Кл.слова (ненормированные):
Gammarus lacustris -- Heat shock proteins 70 (HSP70) -- Nonspecific cellular -- stress-response (NCSR) -- Lactate dehydrogenase -- Diene conjugates -- Schiff -- bases -- Triene conjugates
Аннотация: The previously undescribed dynamics of the heat shock protein HSP70 and subsequent lipid peroxidation products have been assessed alongside lactate dehydrogenase activity for Gammarus lacustris Sars, an amphipod species from the saltwater Lake Shira (Republic of Khakassia). Individuals were exposed to a gradual temperature increase of 1 degrees C/hour (total exposure duration of 26 hours) starting from the mean annual temperature of their habitat (7 degrees C) up to 33 degrees C. A complex of biochemical reactions occurred when saltwater G. lactustris was exposed to the gradual changes in temperature. This was characterized by a decrease in lactate dehydrogenase activity and the launching of lipid peroxidation. The HSP70 level did not change significantly during the entire experiment. In agreement with the concept of oxygen-limited thermal tolerance, an accumulation of the most toxic lipid peroxides (triene conjugates and Schiff bases) in phospholipids occurred at the same time and temperature as the accumulation of lactate. The main criterion overriding the temperature threshold was, therefore, the transition to anaerobiosis, confirmed by the elevated lactate levels as observed in our previous associated study, and by the development of cellular stress, which was expressed by an accumulation of lipid peroxidation products. An earlier hypothesis, based on freshwater individuals of the same species, has been confirmed whereby the increased thermotolerance of G. lacustris from the saltwater lake was caused by differences in energy metabolism and energy supply of nonspecific cellular stress-response mechanisms. With the development of global climate change, these reactions could be advantageous for saltwater G. lacustris. The studied biochemical reactions can be used as biomarkers for the stress status of aquatic organisms when their habitat temperature changes.

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Держатели документа:
Irkutsk State Univ, Inst Biol, Irkutsk, Russia.
Baikal Res Ctr, Irkutsk, Russia.
Belarusian State Univ, Int Sakharov Environm Inst, Minsk, BELARUS.
SB RAS, Inst Biophys, Krasnoyarsk Res Ctr, Krasnoyarsk, Russia.
Siberian Fed Univ, Krasnoyarsk, Russia.

Доп.точки доступа:
Vereshchagina, Kseniya; Kondrateva, Elizaveta; Axenov-Gribanov, Denis; Shatilina, Zhanna; Khomich, Andrey; Bedulina, Daria; Zadereev, Egor; Timofeyev, Maxim; Russian Science Foundation [17-14-01063]; Russian Foundation for Basic Research [16-34-00687, 16-34-60060, 17-34-50012]; Goszadanie project joint program of DAAD [6.9654.2017/8.9]; Ministry of education and Science M. Lomonosov [6.12735.2018/12.2]; Lake Baikal Foundation [FOB_02-3/05]

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20.

The Ca2+-Regulated Photoprotein Obelin as a Target for the RNA Aptamer Selection / V. V. Krasitskaya [et al.] // Russ. J. Bioorg. Chem. - 2018. - Vol. 44, Is. 3. - P296-301, DOI 10.1134/S1068162018030093 . - ISSN 1068-1620
Кл.слова (ненормированные):
2'-fluoro-RNA -- in vitro selection -- RNA aptamers -- Са2+-regulated photoprotein obelin
Аннотация: A variant of the Ca2+-regulated photoprotein obelin elongated with a hexahistidine peptide from the N-terminus was developed and studied. After immobilization on a metal-affine sorbent, the hybrid protein was applied as a target for the in vitro selection of RNA aptamers. According to the data of bioluminescent solid-phase microanalysis, the selection was shown to enrich the RNA library with obelin-affine molecules. © 2018, Pleiades Publishing, Ltd.

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Держатели документа:
Institute of Biophysics Siberian Branch, Russian Academy of Sciences, FRC Krasnoyarsk Science Center, Krasnoyarsk, Russian Federation
Institute of Chemical Biology and Fundamental Medicine, Siberian Branch, Russian Academy of Sciences, Novosibirsk, Russian Federation

Доп.точки доступа:
Krasitskaya, V. V.; Davydova, A. S.; Vorobjeva, M. A.; Frank, L. A.

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