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1.


   
    Violet bioluminescence and fast kinetics from W92F obelin: Structure-based proposals for the bioluminescence triggering and the identification of the emitting species [Text] / E. S. Vysotski [et al.] // Biochemistry. - 2003. - Vol. 42, Is. 20. - P6013-6024, DOI 10.1021/bi027258h. - Cited References: 45 . - ISSN 0006-2960
РУБ Biochemistry & Molecular Biology
Рубрики:
RAY CRYSTALLOGRAPHIC ANALYSIS
   PHOTOPROTEIN AEQUORIN

   ANGSTROM RESOLUTION

   RECOMBINANT OBELIN

   CALCIUM

   LUMINESCENCE

   LONGISSIMA

   EVOLUTION

   PROTEINS

   COELENTERAZINE

Аннотация: Obelin from the hydroid Obelia longissima and aequorin are members of a subfamily of Ca2+-regulated photoproteins that is a part of the larger EF-hand calcium binding protein family. On the addition of Ca2+, obelin generates a blue bioluminescence emission (lambda(max) = 485 nm) as the result of the oxidative decarboxylation of the bound substrate, coelenterazine. The W92F obelin mutant is noteworthy because of the unusually high speed with which it responds to sudden changes of [Ca2+] and because it emits violet light rather than blue due to a prominent band with lambda(max) = 405 nm. Increase of pH in the range from 5.5 to 8.5 and using D2O both diminish the contribution of the 405 nm band, indicating that excited state proton transfer is involved. Fluorescence model studies have suggested the origin of the 485 nm emission as the excited state of an anion of coelenteramide, the bioluminescence reaction product, and 405 nm from the excited neutral state. Assuming that the dimensions of the substrate binding cavity do not change during the excited state formation, a His22 residue within hydrogen bonding distance to the 6-(p-hydroxy)-phenyl group of the excited coelenteramide is a likely candidate for accepting the phenol proton to produce an ion-pair excited state, in support of recent suggestions for the bioluminescence emitting state. The proton transfer could be impeded by removal of the Trp92 H-bond, resulting in strong enhancement of a 405 nm band giving the violet color of bioluminescence. Comparative analysis of 3D structures of the wild-type (WT) and W92F obelins reveals that there are structural displacements of certain key Ca2+-ligating residues in the loops of the two C-terminal EF hands as well as clear differences in hydrogen bond networks in W92F. For instance, the hydrogen bond between the side-chain oxygen atom of Asp 169 and the main-chain nitrogen of Arg112 binds together the incoming alpha-helix of loop III and the exiting cc-helix of loop IV in WT, providing probably concerted changes in these EF hands on calcium binding. But this linkage is not found in W92F obelin. These differences apparently do not change the overall affinity to calcium of W92F obelin but may account for the kinetic differences between the WT and mutant obelins. From analysis of the hydrogen bond network in the coelenterazine binding cavity, it is proposed that the trigger for bioluminescence reaction in these Ca2+-regulated photoproteins may be a shift of the hydrogen bond donor-acceptor separations around the coelenterazine-2-hydroperoxy substrate, initiated by small spatial adjustment of the exiting a-helix of loop IV.

Держатели документа:
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
Univ Georgia, Dept Chem, Athens, GA USA
RAS, SB, Photobiol Lab, Inst Biophys, Krasnoyarsk, Russia
Univ Washington, Friday Harbor Labs, Seattle, WA 98195 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Vysotski, E.S.; Liu, Z.J.; Markova, S.V.; Blinks, J.R.; Deng, L...; Frank, L.A.; Herko, M...; Malikova, N.P.; Rose, J.P.; Wang, B.C.; Lee, J...

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2.


   
    Usage of different neural networks in identification of plant types / S. Bartsev, Y. Ivanova, M. Saltykov // IOP Conference Series: Materials Science and Engineering : Institute of Physics Publishing, 2020. - Vol. 734: 2nd International Scientific Conference on Advanced Technologies in Aerospace, Mechanical and Automation Engineering, MIST: Aerospace 2019 (18 November 2019 through 21 November 2019, ) Conference code: 157461, Is. 1. - Ст. 012097, DOI 10.1088/1757-899X/734/1/012097
Аннотация: Since introduction of neural networks into remote sensing they demonstrate good efficiency in remote sensing data analysis. This work is devoted to processing of multispectral (12 bands) images from Sentinel-2(A, B) satellites. Satellite images of areas in Krasnoyarsk Region and Khakassia with known vegetation types are used as task books to train neural networks. Trained neural networks have been reduced to determine which bands are significant for vegetation type identification. Reduction of trained neural network show that vegetation type can be determined from only four infrared bands without significant loses in performance in comparison with non-reduced neural network. © Published under licence by IOP Publishing Ltd.

Scopus
Держатели документа:
Institute of Biophysics FRC KSC SB RAS, Akademgorodok 50/50, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Bartsev, S.; Ivanova, Y.; Saltykov, M.

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3.


   
    The Restoration Dynamics of Fallow Vegetation in the Steppe Zone of the Khakassia Republic Based on Terrain and Satellite Data / I. Y. Botvich, T. M. Zorkina // Biophysics. - 2019. - Vol. 64, Is. 2. - P309-315, DOI 10.1134/S0006350919020039 . - ISSN 0006-3509
Кл.слова (ненормированные):
fallow lands -- long-term variability (structure -- MODIS -- NDVI -- phytomass) -- projective cover -- restoration of natural vegetation -- satellite and terrain research methods
Аннотация: Abstract: The dynamics and specific features of the restoration of forbs–grass–wormwood and wormwood–grass phytocoenoses on fallow lands in the Altai region, the Republic of Khakassia, were determined on the basis of terrain and satellite data. The species composition, structure, and phytomass of the phytocoenoses were revealed. A gradual formation of structural elements of steppe communities in the studied areas was determined. This work showed the usefulness of time series of satellite data on the NDVI (Normalized Difference Vegetation Index) obtained with the use of MODIS (Moderate Resolution Imaging Spectroradiometer) for the study of specific features of restored fallows. In general the biological parameters, projective cover, and phytomass determine the value of the NDVI. Interannual NDVI variability reflects the rate and time period of fallow restoration. From a certain point, the parameters increased and became close to the steppe (control variant). It has been revealed that not only abiotic factors (climate and soils), but also biotic parameters (grazing and recreational load) affect the NDVI. In this connection, the duration of restoration stages does not always correspond to the published data. They vary under different conditions. Climatic data of the Abakan meteorological station (index 29862 in the network of the World Meteorological Organization) for the period from 2000 to 2017 were statistically treated. The long-term annual average norms of temperatures and precipitation amounts (year and month) for the World Meteorological Organization base period of 1961–1990 were calculated. The dynamics of the temperature and precipitation, using long-term series of data, has been analyzed. © 2019, Pleiades Publishing, Inc.

Scopus,
Смотреть статью
Держатели документа:
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Division of Federal Research Center Krasnoyarsk Scientific Center, Siberian Branch, Russian Academy of Sciences, Krasnoyarsk, 660036, Russian Federation
Cherepnin Herbarium, Astaf’ev Krasnoyarsk State Pedagogical University, Krasnoyarsk, 660049, Russian Federation

Доп.точки доступа:
Botvich, I. Y.; Zorkina, T. M.

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4.


   
    The interaction of C-terminal Tyr208 and Tyr13 of the first α-helix ensures a closed conformation of ctenophore photoprotein berovin / L. P. Burakova, E. V. Eremeeva, E. S. Vysotski // Photochem. Photobiol. Sci. - 2020. - Vol. 19, Is. 3. - P313-323, DOI 10.1039/c9pp00436j . - ISSN 1474-905X
Кл.слова (ненормированные):
Amino acids -- Bioluminescence -- Conformations -- Phosphorescence -- Amino acid residues -- Amino acid sequence -- Hydrogen bond networks -- Hydromedusan -- Internal cavities -- Phenyl rings -- Photoproteins -- Pi interactions -- Hydrogen bonds
Аннотация: Light-sensitive Ca2+-regulated photoprotein berovin is responsible for the bioluminescence of the ctenophore Beroe abyssicola. It shares many properties of hydromedusan photoproteins although the degree of identity of its amino acid sequence with those of photoproteins is low. There is a hydrogen bond between C-terminal Pro and Arg situated in the N-terminal ?-helix of hydromedusan photoproteins that supports a closed conformation of the internal cavity of the photoprotein molecule with bound 2-hydroperoxycoelenterazine. The C- and N-terminal hydrogen bond network is necessary to properly isolate the photoprotein active site from the solvent and consequently to provide a high quantum yield of the bioluminescence reaction. In order to find out which berovin residues perform the same function we modified the N- and C-termini of the protein by replacing or deleting various amino acid residues. The studies on berovin mutants showed that the interaction between C-terminal Tyr208 and Tyr13 localized in the first ?-helix of the photoprotein is important for the stabilization and proper orientation of the oxygenated coelenterazine adduct within the internal cavity as well as for supporting the closed photoprotein conformation. We also suggest that the interplay between Tyr residues in ctenophore photoproteins occurs rather through the ?-? interaction of their phenyl rings than through hydrogen bonds as in hydromedusan photoproteins. This journal is © The Royal Society of Chemistry and Owner Societies.

Scopus
Держатели документа:
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center Krasnoyarsk Science Center SB RAS, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Burakova, L. P.; Eremeeva, E. V.; Vysotski, E. S.

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5.


   
    The interaction of C-terminal Tyr208 and Tyr13 of the first alpha-helix ensures a closed conformation of ctenophore photoprotein berovin / L. P. Burakova, E. V. Eremeeva, E. S. Vysotski // Photochem. Photobiol. Sci. - 2020. - Vol. 19, Is. 3. - P313-323, DOI 10.1039/c9pp00436j. - Cited References:49. - This work was supported by grant 17-04-00764 of the Russian Foundation for Basic Research. . - ISSN 1474-905X. - ISSN 1474-9092
РУБ Biochemistry & Molecular Biology + Biophysics + Chemistry, Physical
Рубрики:
LIGHT-SENSITIVE PHOTOPROTEIN
   GREEN FLUORESCENT PROTEIN

Аннотация: Light-sensitive Ca2+-regulated photoprotein berovin is responsible for the bioluminescence of the ctenophore Beroe abyssicola. It shares many properties of hydromedusan photoproteins although the degree of identity of its amino acid sequence with those of photoproteins is low. There is a hydrogen bond between C-terminal Pro and Arg situated in the N-terminal alpha-helix of hydromedusan photoproteins that supports a closed conformation of the internal cavity of the photoprotein molecule with bound 2-hydroperoxycoelenterazine. The C- and N-terminal hydrogen bond network is necessary to properly isolate the photoprotein active site from the solvent and consequently to provide a high quantum yield of the bioluminescence reaction. In order to find out which berovin residues perform the same function we modified the N- and C-termini of the protein by replacing or deleting various amino acid residues. The studies on berovin mutants showed that the interaction between C-terminal Tyr208 and Tyr13 localized in the first alpha-helix of the photoprotein is important for the stabilization and proper orientation of the oxygenated coelenterazine adduct within the internal cavity as well as for supporting the closed photoprotein conformation. We also suggest that the interplay between Tyr residues in ctenophore photoproteins occurs rather through the pi-pi interaction of their phenyl rings than through hydrogen bonds as in hydromedusan photoproteins.

WOS
Держатели документа:
RAS, SB, Photobiol Lab, Inst Biophys,Fed Res Ctr,Krasnoyarsk Sci Ctr, Krasnoyarsk, Russia.

Доп.точки доступа:
Burakova, Ludmila P.; Eremeeva, Elena V.; Vysotski, Eugene S.; Vysotski, Eugene; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [17-04-00764]

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6.


   
    Role of key residues of obelin in coelenterazine binding and conversion into 2-hydroperoxy adduct [Text] / E. V. Eremeeva [et al.] // J. Photochem. Photobiol. B-Biol. - 2013. - Vol. 127. - P133-139, DOI 10.1016/j.jphotobiol.2013.08.012. - Cited References: 65. - The work was supported by RFBR grant 12-04-00131, by the Programs of the Government of Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.0058), "Molecular and Cellular Biology" of RAS, President of Russian Federation "Leading science school" (grant 3951.2012.4). E.V.E. was supported by Wageningen University Sandwich PhD-Fellowship Program. . - ISSN 1011-1344
РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
CA2+-REGULATED PHOTOPROTEINS
   SEQUENCE-ANALYSIS

   CRYSTAL-STRUCTURE

   APO-OBELIN

   CA2+-BINDING PHOTOPROTEIN

   VIOLET BIOLUMINESCENCE

   AEQUORIN REGENERATION

   ANGSTROM RESOLUTION

   RECOMBINANT OBELIN

   MNEMIOPSIS-LEIDYI

Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Obelin -- Aequorin -- Photoprotein
Аннотация: Bioluminescence of a variety of marine organisms is caused by monomeric Ca2+-regulated photoproteins, to which a peroxy-substituted coelenterazine, 2-hydroperoxycoelenterazine, is firmly bound. From the spatial structure the side chains of Tyr138, His175, Trp179, and Tyr190 of obelin are situated within the substrate-binding pocket at hydrogen bond distances with different atoms of the 2-hydroperoxycoelenterazine. Here we characterized several obelin mutants with substitutions of these residues regarding their bioluminescence, coelenterazine binding, and kinetics of active obelin formation. We demonstrate that Tyr138, His175, Trp179, and Tyr190 are all important for coelenterazine activation; substitution of any of these residues leads to significant decrease of the apparent reaction rate. The hydrogen bond network formed by Tyr138, Trp179 and Tyr190 participates in the proper positioning of coelenterazine in the active site and subsequent stabilization of the 2-hydroperoxy adduct of coelenterazine. His175 might serve as a proton shuttle during 2-hydroperoxycoelenterazine formation. (C) 2013 Elsevier B.V. All rights reserved.

WOS
Держатели документа:
[Eremeeva, Elena V.
Markova, Svetlana V.
Vysotski, Eugene S.] Russian Acad Sci, Photobiol Lab, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
[Eremeeva, Elena V.
van Berkel, Willem J. H.] Wageningen Univ, Biochem Lab, NL-6703 HA Wageningen, Netherlands
[Eremeeva, Elena V.
Markova, Svetlana V.
Vysotski, Eugene S.] Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Lab Bioluminescence Biotechnol, Krasnoyarsk 660041, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Eremeeva, E.V.; Markova, S.V.; van Berkel, WJH; Vysotski, E.S.; RFBR [12-04-00131]; Programs of the Government of Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" [11.G34.31.0058]; "Molecular and Cellular Biology" of RAS, President of Russian Federation "Leading science school" [3951.2012.4]; Wageningen University Sandwich PhD-Fellowship Program

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7.


   
    Redquorinxs mutants with enhanced calcium sensitivity and bioluminescence output efficiently report cellular and neuronal network activities / A. Bakayan, S. Picaud, N. P. Malikova [et al.] // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 21. - Ст. 7846. - P1-22, DOI 10.3390/ijms21217846 . - ISSN 1661-6596
Кл.слова (ненормированные):
Aequorin -- Bioluminescence -- BRET -- Calcium sensor -- GPCR assay -- Mutagenesis -- Neuronal network imaging
Аннотация: Considerable efforts have been focused on shifting the wavelength of aequorin Ca2+? dependent blue bioluminescence through fusion with fluorescent proteins. This approach has notably yielded the widely used GFP?aequorin (GA) Ca2+ sensor emitting green light, and tdTomato-aequorin (Redquorin), whose bioluminescence is completely shifted to red, but whose Ca2+ sensitivity is low. In the present study, the screening of aequorin mutants generated at twenty?four amino acid positions in and around EF?hand Ca2+?binding domains resulted in the isolation of six aequorin single or double mutants (AequorinXS) in EF2, EF3, and C?terminal tail, which exhibited markedly higher Ca2+ sensitivity than wild?type aequorin in vitro. The corresponding Redquorin mutants all showed higher Ca2+ sensitivity than wild?type Redquorin, and four of them (RedquorinXS) matched the Ca2+ sensitivity of GA in vitro. RedquorinXS mutants exhibited unaltered thermostability and peak emission wavelengths. Upon stable expression in mammalian cell line, all RedquorinXS mutants reported the activation of the P2Y2 receptor by ATP with higher sensitivity and assay robustness than wt?Redquorin, and one, RedquorinXS?Q159T, outperformed GA. Finally, wide?field bioluminescence imaging in mouse neocortical slices showed that RedquorinXS?Q159T and GA similarly reported neuronal network activities elicited by the removal of extracellular Mg2+. Our results indicate that RedquorinXS?Q159T is a red light?emitting Ca2+ sensor suitable for the monitoring of intracellular signaling in a variety of applications in cells and tissues, and is a promising candidate for the transcranial monitoring of brain activities in living mice. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.

Scopus
Держатели документа:
Institut de Neurobiologie Alfred Fessard, UPR 3294, Centre National de la Recherche Scientifique (CNRS), Avenue de la Terrasse, Gif?sur?Yvette, 91198, France
BioEmergences Unit, CNRS USR 3695, Universite Paris?Saclay, Avenue de la Terrasse, Gif?sur?Yvette, 91198, France
Neuroscience Paris Seine ? Institut de Biologie Paris Seine (NPS ? IBPS), CNRS, UMR8246, INSERM U1130, Sorbonne Universite UM119, Paris, 75005, France
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Bakayan, A.; Picaud, S.; Malikova, N. P.; Tricoire, L.; Lambolez, B.; Vysotski, E. S.; Peyrieras, N.

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8.


   
    RedquorinXS Mutants with Enhanced Calcium Sensitivity and Bioluminescence Output Efficiently Report Cellular and Neuronal Network Activities / A. Bakayan, S. Picaud, N. P. Malikova [et al.] // Int. J. Mol. Sci. - 2020. - Vol. 21, Is. 21. - Ст. 7846, DOI 10.3390/ijms21217846. - Cited References:53. - This work was supported by grants from Centre National de la Recherche Scientifique (AAP Prematuration CNRS 2016, to A.B. and N.P.; equipment transfer to S.P. and B.L.), from Agence Nationale de la Recherche (AAP Prematuration FCS/IDEX Paris Saclay, to A.B. and N.P., France BioImaging infrastructure ANR-10-INBS-04, ANR-11-EQPX-029 to N.P.), from Fondation pour la Recherche sur le Cerveau/Rotary Club de France (B.L.), and from RFBR (project number 20-04-00085 to N.P.M. and E.S.V.). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. . - ISSN 1422-0067
РУБ Biochemistry & Molecular Biology + Chemistry, Multidisciplinary
Рубрики:
IN-VIVO
   PHOTOPROTEIN AEQUORIN

   CA2+-REGULATED PHOTOPROTEINS

   SPREADING

Кл.слова (ненормированные):
bioluminescence -- aequorin -- calcium sensor -- BRET -- mutagenesis -- GPCR -- assay -- neuronal network imaging
Аннотация: Considerable efforts have been focused on shifting the wavelength of aequorin Ca2+-dependent blue bioluminescence through fusion with fluorescent proteins. This approach has notably yielded the widely used GFP-aequorin (GA) Ca2+ sensor emitting green light, and tdTomato-aequorin (Redquorin), whose bioluminescence is completely shifted to red, but whose Ca2+ sensitivity is low. In the present study, the screening of aequorin mutants generated at twenty-four amino acid positions in and around EF-hand Ca2+-binding domains resulted in the isolation of six aequorin single or double mutants (AequorinXS) in EF2, EF3, and C-terminal tail, which exhibited markedly higher Ca2+ sensitivity than wild-type aequorin in vitro. The corresponding Redquorin mutants all showed higher Ca2+ sensitivity than wild-type Redquorin, and four of them (RedquorinXS) matched the Ca2+ sensitivity of GA in vitro. RedquorinXS mutants exhibited unaltered thermostability and peak emission wavelengths. Upon stable expression in mammalian cell line, all RedquorinXS mutants reported the activation of the P2Y2 receptor by ATP with higher sensitivity and assay robustness than wt-Redquorin, and one, RedquorinXS-Q159T, outperformed GA. Finally, wide-field bioluminescence imaging in mouse neocortical slices showed that RedquorinXS-Q159T and GA similarly reported neuronal network activities elicited by the removal of extracellular Mg2+. Our results indicate that RedquorinXS-Q159T is a red light-emitting Ca2+ sensor suitable for the monitoring of intracellular signaling in a variety of applications in cells and tissues, and is a promising candidate for the transcranial monitoring of brain activities in living mice.

WOS
Держатели документа:
Ctr Natl Rech Sci CNRS, Inst Neurobiol Alfred Fessard, UPR 3294, Ave Terrasse, F-91198 Gif Sur Yvette, France.
Univ Paris Saclay, BioEmergences Unit, CNRS, USR 3695, Ave Terrasse, F-91198 Gif Sur Yvette, France.
Sorbonne Univ, Inst Biol Paris Seine NPS IBPS, INSERM, Neurosci Paris Seine,CNRS,UMR8246,U1130,UM119, F-75005 Paris, France.
Inst Biophys SB RAS, Fed Res Ctr, Photobiol Lab, Krasnoyarsk Sci Ctr SB RAS, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Bakayan, Adil; Picaud, Sandrine; Malikova, Natalia P.; Tricoire, Ludovic; Lambolez, Bertrand; Vysotski, Eugene S.; Peyrieras, Nadine; Vysotski, Eugene; Centre National de la Recherche ScientifiqueCentre National de la Recherche Scientifique (CNRS); Agence Nationale de la RechercheFrench National Research Agency (ANR) [ANR-10-INBS-04, ANR-11-EQPX-029]; Fondation pour la Recherche sur le Cerveau/Rotary Club de France; RFBRRussian Foundation for Basic Research (RFBR) [20-04-00085]

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9.


   
    Recurrent and multi-layer neural networks playing Even-Odd": Reflection against regression / S. Bartsev, G. Markova // IOP Conference Series: Materials Science and Engineering : Institute of Physics Publishing, 2020. - Vol. 734: 2nd International Scientific Conference on Advanced Technologies in Aerospace, Mechanical and Automation Engineering, MIST: Aerospace 2019 (18 November 2019 through 21 November 2019, ) Conference code: 157461, Is. 1. - Ст. 012109, DOI 10.1088/1757-899X/734/1/012109
Аннотация: Reflection understood as an internal representation of the external world by the subject is the key property of consciousness. In a refined form this property is manifested in reflective games. To win a reflective game a player has to use reflection of strictly one rank higher than the opponent. So it can be assumed that there are only two game modes - when only one player uses reflection and wins and when both players use reflection but one of them chooses incorrect reflection rank. The option of random move selection is not considered since firstly, starting the game for a draw is strange, and secondly, it is technically impossible to make random moves without a special device. Experiments with recurrent neural networks playing with each other showed that the entire set of game patterns (time series of the game score) is split into two sharply different groups that can be associated with two modes mentioned above. Experiments, in which a multilayer neural network, which is basically incapable of reflection, played against a recurrent neural network, showed that a recurrent neural network has a clear advantage winning confidently in more than 90% of the games. At the same time game patterns demonstrate splitting into two sharply different groups as was observed in experiments with the game of two recurrent neural networks and in the reflexive game of living people. © Published under licence by IOP Publishing Ltd.

Scopus
Держатели документа:
Institute of Biophysics SB RAS, Federal Research Center, Krasnoyarsk Scientific Center SB RAS, 50, Akademgorodok, Krasnoyarsk, 660036, Russian Federation
Siberian Federal University, 79 Svobodny pr., Krasnoyarsk, 660041, Russian Federation

Доп.точки доступа:
Bartsev, S.; Markova, G.

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10.


   
    Production of a Composite Based on Alumina Nanofibers and Detonation Nanodiamonds for Creating Phenol Indication Systems / N. O. Ronzhin, E. D. Posokhina, E. V. Mikhlina [et al.] // Dokl. Chem. - 2019. - Vol. 489, Is. 1. - P267-271, DOI 10.1134/S001250081911003X . - ISSN 0012-5008
Аннотация: Abstract: A composite of alumina nanofibers (ANF) and modified detonation nanodiamonds (MDND) was produced by mixing aqueous suspensions of the components in a weight ratio of 5 : 1 with subsequent incubation of the mixture for 15 min at 32°C. It was assumed that the formation of the composite is ensured by the difference of the zeta potentials of the components, which is negative for MDND and positive for ANF. Vacuum filtration of the mixture through a fluoroplastic filter (pore diameter 0.6 ?m) formed disks 40 mm in diameter, which were then heat-treated at 300°C to impart structural stability to the composite. Scanning electron microscopy detected that the obtained composite has a network structure, in which MDND particles are distributed over the surface of ANF. It was determined that the MDND particles incorporated in the composite catalyze the phenol–4-aminoantipyrine–H2O2 oxidative azo coupling reaction to form a colored product (quinoneimine). The applicability of the composite to repeated phenol detection in aqueous samples was demonstrated. © 2019, Pleiades Publishing, Ltd.

Scopus
Держатели документа:
Institute of Biophysics, Krasnoyarsk Scientific Center, Siberian Branch, Russian Academy of Sciences, AkademgorodokKrasnoyarsk, 660036, Russian Federation
Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Institute of Computational Modeling, Krasnoyarsk Scientific Center, Siberian Branch, Russian Academy of Sciences, AkademgorodokKrasnoyarsk, 660036, Russian Federation
Krasnoyarsk Scientific Center, Siberian Branch, Russian Academy of Sciences, AkademgorodokKrasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Ronzhin, N. O.; Posokhina, E. D.; Mikhlina, E. V.; Simunin, M. M.; Nemtsev, I. V.; Ryzhkov, I. I.; Bondar, V. S.

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11.


   
    Production of a Composite Based on Alumina Nanofibers and Detonation Nanodiamonds for Creating Phenol Indication Systems / N. O. Ronzhin, E. D. Posokhina, E. V. Mikhlina [et al.] // Dokl. Chem. - 2019. - Vol. 489. - P267-271, DOI 10.1134/S001250081911003X. - Cited References:13. - This work was supported by the Russian Foundation for Basic Research (project no. 18-29-19078 mk). . - ISSN 0012-5008. - ISSN 1608-3113
РУБ Chemistry, Multidisciplinary
Рубрики:
NANOPARTICLES
   GRAPHENE

Аннотация: A composite of alumina nanofibers (ANF) and modified detonation nanodiamonds (MDND) was produced by mixing aqueous suspensions of the components in a weight ratio of 5 : 1 with subsequent incubation of the mixture for 15 min at 32 degrees C. It was assumed that the formation of the composite is ensured by the difference of the zeta potentials of the components, which is negative for MDND and positive for ANF. Vacuum filtration of the mixture through a fluoroplastic filter (pore diameter 0.6 mu m) formed disks 40 mm in diameter, which were then heat-treated at 300 degrees C to impart structural stability to the composite. Scanning electron microscopy detected that the obtained composite has a network structure, in which MDND particles are distributed over the surface of ANF. It was determined that the MDND particles incorporated in the composite catalyze the phenol-4-aminoantipyrine-H2O2 oxidative azo coupling reaction to form a colored product (quinoneimine). The applicability of the composite to repeated phenol detection in aqueous samples was demonstrated.

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Держатели документа:
Russian Acad Sci, Siberian Branch, Krasnoyarsk Sci Ctr, Inst Biophys, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
Russian Acad Sci, Siberian Branch, Inst Computat Modeling, Krasnoyarsk Sci Ctr, Krasnoyarsk 660036, Russia.
Russian Acad Sci, Siberian Branch, Krasnoyarsk Sci Ctr, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Ronzhin, N. O.; Posokhina, E. D.; Mikhlina, E. V.; Simunin, M. M.; Nemtsev, I. V.; Ryzhkov, I. I.; Bondar, V. S.; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [18-29-19078 mk]

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12.


   
    Predicting the state of the Earth's ozone layer for different time intervals with the use of neural networks [Text] / V. B. Kashkin, Y. P. Lankin, I. Y. Sakash // Izv. Atmos. Ocean. Phys. - 2005. - Vol. 41, Is. 4. - P. 469-475. - Cited References: 10 . - ISSN 0001-4338
РУБ Meteorology & Atmospheric Sciences + Oceanography
Рубрики:
ERRORS
Аннотация: The problems of studying and simulating the Earth's ozone layer are discussed. It is shown that the construction of models for the total ozone content (TOC) in the stratosphere with the use of neural networks is promising. The neural-network algorithm used is described. TOC forecasts for different time periods are made using neuronetwork models.

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Держатели документа:
Krasnoyarsk State Tech Univ, Krasnoyarsk 660074, Russia
Russian Acad Sci, Inst Biophys, Siberian Div, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kashkin, V.B.; Lankin, Y.P.; Sakash, I.Y.

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13.


   
    Picosecond Fluorescence Relaxation Spectroscopy of the Calcium-Discharged Photoproteins Aequorin and Obelin [Text] / B. . van Oort [et al.] // Biochemistry. - 2009. - Vol. 48, Is. 44. - P10486-10491, DOI 10.1021/bi901436m. - Cited References: 33. - This work was supported by NATO Collaborative Linkage Grant No 979229,Grants of SB RAS and RFBR 09-04-12-022, MCB program of RAS BvO was supported by 'Stichung voor Fundamenteel Onderzock der Materic (FOM)', which is financially supported by the NWO. and by I Rubicon grant of NWO E V E was supported by Wageningen University Sandwich Ph D-Fellowship program S P L was supported by Wageningen University Sandwich Ph D.-Fellowship program, European Community Marie Curie Research Training Network MRTN-CT-2005-019481 (From FLIM to FLIN), and Computational Science Gram 635 000 014 from the netherlands Organization for Scientific Research . - ISSN 0006-2960
РУБ Biochemistry & Molecular Biology
Рубрики:
CA2+-REGULATED PHOTOPROTEINS
   VIOLET BIOLUMINESCENCE

   ANGSTROM RESOLUTION

   RECOMBINANT OBELIN

   CRYSTAL-STRUCTURE

   W92F OBELIN

   COELENTERAZINE

   MECHANISM

   EXPRESSION

   PROTEINS

Аннотация: Addition of calcium tons to the Ca(2+)-regulated photoproteins, such its aequorin and obelin, produces it blue bioluminescence originating from fluorescence transition of the protein-bound product coelenteramide. The kinetics of several transient fluorescent species of the bound coelenteramide is resolved after picosecond-laser excitation and streak camera detection. The Initially formed spectral distributions at picosecond-times are broad, evidently comprised of two contributions, One at higher energy (similar to 25 000 cm(-1)) assigned as from the Ca(2+)-discharged photoprotein-bound coelenteramide in its neutral state. This component decays much more rapidly (t(1/2) similar to 2 ps) in the case of the Ca(2+)-discharged obelin than aequorin (t(1/2) similar to 30 ps). The Second component at lower energy shows several intermediates in the 150-500 ps miles. with it Final species having spectral maxima 19 400 cm(-1), bound to Ca(2+)-discharged obelin. and 2 1300 cm(-1), bound to Ca(2+)-discharged aequorin, and both have it fluorescence decay lifetime of 4 ns It is proposed that the rapid kinetics of these fluorescence transients oil the picosecond time scale, correspond to times For relaxation of the protein Structural environment of the binding cavity

Держатели документа:
[Lee, John] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
[van Oort, Bart
Koehorst, Rob B. M.
Laptenok, Sergey P.
van Amerongen, Herbert] Wageningen Univ, Biophys Lab, NL-6703 HA Wageningen, Netherlands
[Eremeeva, Elena V.
Laptenok, Sergey P.
van Berkel, Willem J. H.
Visser, Antonie J. W. G.] Wageningen Univ, Biochem Lab, NL-6703 HA Wageningen, Netherlands
[Koehorst, Rob B. M.
van Amerongen, Herbert
Visser, Antonie J. W. G.] Wageningen Univ, Microspect Ctr, NL-6703 HA Wageningen, Netherlands
[Eremeeva, Elena V.
Malikova, Natalia P.
Markova, Svetlana V.
Vysotski, Eugene S.] Russian Acad Sci, Inst Biophys, Photobiol Lab, Siberian Branch, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
van Oort, B...; Eremeeva, E.V.; Koehorst, RBM; Laptenok, S.P.; van Amerongen, H...; van Berkel, WJH; Malikova, N.P.; Markova, S.V.; Vysotski, E.S.; Visser, AJWG; Lee, J...; NATO Collaborative Linkage [979229]; RFBR [09-04-12-022]; 'Stichung voor Fundamenteel Onderzock der Materic (FOM)'; NWO; Wageningen University; European Community Marie Curie Research Training Network [MRTN-CT-2005-019481]; netherlands Organization [635 000 014]

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14.


   
    Phylogeny of Salmonoid Fishes (Salmonoidei) Based on mtDNA COI Gene Sequences (Barcoding) / V. S. Artamonova [et al.] // Contemp. Probl. Ecol. - 2018. - Vol. 11, Is. 3. - P271-285, DOI 10.1134/S1995425518030022. - Cited References:102. - We are very grateful to colleagues who helped collect samples: E.G. Berestovskii, I.N. Bolotov, E.A. Borovikova, I.V. Vikhrev, L.A. Glushchenko, V.V. Ignatenko, D.P. Karabanov, A.P. Novoselov, V.M. Spitsyn, V.A. Shirokov, and I.L. Shchurov; employees of Trout Hatchery "Adler", the Federal Breeding and Genetic Center for Fish Culture, and Vygsky and Kemsky fish hatcheries; and residents of Barabash-Levada, Len-lu, and Chupa settlements. We also thank S.S. Alekseev for identifying sharp-snouted and blunt-snouted lenoks. This work was supported by the Russian Science Foundation, project no. 16-14-10001. . - ISSN 1995-4255. - ISSN 1995-4263
РУБ Ecology
Рубрики:
MOLECULAR DATING ANALYSIS
   GROWTH-HORMONE INTRONS

   SALMONIFORMES

Кл.слова (ненормированные):
evolution -- network -- molecular clock -- amino acid sequence -- reproductive -- isolation -- immobilization -- fishes
Аннотация: We have analyzed the partial sequences of the mitochondrial COI gene along with the amino acid sequences of cytochrome oxidase subunit I, encoded by this gene region, in representatives of 11 genera of salmonoid fish. For amino acid sequences, two alternative networks are constructed with outgroups represented by either Esocoidei or Osmeroidei as the supposed ancestral groups. This way, Osmeroidei appear to be closer to the salmonoid fish than Esocoidei, and their presence in the network as an outgroup explains the available data on the morphology and karyology of salmonoids much better. A number of the results of this study are fundamentally new. In particular, the slowing down of the molecular evolution of the grayling (Thymallidae) is shown. We conclude that the charr (Salvelinus) is one of the modern genera of salmonoids closest to their ancestor. The hypothesis of the phylogenetic proximity of the genera Brachymystax, Hucho, and Salmo has been confirmed. We also discuss the possibility that it is namely the changes in the amino acid sequence of cytochrome oxidase subunit I that lead to postzygotic reproductive isolation between taxa.

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Держатели документа:
Russian Acad Sci, Severtsov Inst Ecol & Evolut, Moscow 119071, Russia.
Russian Acad Sci, Siberian Branch, Krasnoyarsk Sci Ctr, Inst Biophys, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Artamonova, V. S.; Kolmakova, O. V.; Kirillova, E. A.; Makhrov, A. A.; Russian Science Foundation [16-14-10001]

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15.


   
    Neural networks playing 'matching pennies' with each other: Reproducibility of game dynamics / T. Dolgova, S. Bartsev // IOP Conference Series: Materials Science and Engineering : Institute of Physics Publishing, 2019. - Vol. 537: International Workshop on Advanced Technologies in Material Science, Mechanical and Automation Engineering - MIP: Engineering-2019 (4 April 2019 through 6 April 2019, ) Conference code: 149243, Is. 4, DOI 10.1088/1757-899X/537/4/042002
Кл.слова (ненормированные):
Condensed matter physics -- Engineering -- Industrial engineering -- Materials science -- Cognitive functions -- Dynamic patterns -- Essential features -- Meta strategies -- Neural correlates of consciousness -- Neuron excitation -- Qualitative differences -- Reproducibilities -- Recurrent neural networks
Аннотация: Reflection is an essential feature of consciousness and possibly the single most important one. This fact allows us to simplify the objective of the concept of 'neural correlates of consciousness' and to focus investigations on reflection itself. Reflexive games are the concentrated and pure embodiment of reflection manifestation without the addition of other higher cognitive functions. In this paper, we use the game 'matching pennies' ("Odd-Even") in order to trace the strategies and possible patterns of recurrent neural network operation. Experimental results show the splitting of all considered game patterns into two groups. A significant difference was observed in these groups of patterns, indicating a qualitative difference in game dynamics apparently due to the qualitatively different dynamic patterns of neuron excitations of the networks. A similar splitting of all players into two groups was found by other authors for human players, which differ in terms of the reflection availability. By this, we can assume that one of the causes of the splitting is that the presence of reflection in a particular group of recurrent neural networks dramatically changes the game meta-strategy. © Published under licence by IOP Publishing Ltd.

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Держатели документа:
Siberian Federal University, 2 79 Svobodny pr., Krasnoyarsk, 660041, Russian Federation
Institute of Biophysics SB RAS, Federal Research Center, Krasnoyarsk Scientific Center SB RAS, 50, Akademgorodok, Krasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Dolgova, T.; Bartsev, S.

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16.


   
    Neural networks playing 'matching pennies' with each other: reproducibility of game dynamics / T. Dolgova, S. Bartsev // INTERNATIONAL WORKSHOP ADVANCED TECHNOLOGIES IN MATERIAL SCIENCE, : IOP PUBLISHING LTD, 2019. - Vol. 537: International Workshop on Advanced Technologies in Material Science, (APR 04-06, 2019, Krasnoyarsk, RUSSIA). - Ст. 042002. - (IOP Conference Series-Materials Science and Engineering), DOI 10.1088/1757-899X/537/4/042002. - Cited References:18 . -
РУБ Engineering, Mechanical + Materials Science, Multidisciplinary
Рубрики:
REPRESENTATIONS
   CONSCIOUSNESS

Аннотация: Reflection is an essential feature of consciousness and possibly the single most important one. This fact allows us to simplify the objective of the concept of 'neural correlates of consciousness' and to focus investigations on reflection itself. Reflexive games are the concentrated and pure embodiment of reflection manifestation without the addition of other higher cognitive functions. In this paper, we use the game 'matching pennies' ("Odd-Even") in order to trace the strategies and possible patterns of recurrent neural network operation. Experimental results show the splitting of all considered game patterns into two groups. A significant difference was observed in these groups of patterns, indicating a qualitative difference in game dynamics apparently due to the qualitatively different dynamic patterns of neuron excitations of the networks. A similar splitting of all players into two groups was found by other authors for human players, which differ in terms of the reflection availability. By this, we can assume that one of the causes of the splitting is that the presence of reflection in a particular group of recurrent neural networks dramatically changes the game meta-strategy.

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Держатели документа:
Siberian Fed Univ, 79 Svobodny Pr, Krasnoyarsk 660041, Russia.
RAS, SB, Inst Biophys, Fed Res Ctr,Krasnoyarsk Sci Ctr, 50 Akad Gorodok, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Dolgova, T.; Bartsev, S.

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17.


   
    Naturally deducing estimate for the coefficient of CELSS closure [Text] / S. I. Bartsev ; ed. M Nelson [et al.] // SPACE LIFE SCIENCES: CLOSED ARTIFICIAL ECOSYSTEMS AND LIFE SUPPORT SYSTEMS. Ser. ADVANCES IN SPACE RESEARCH : PERGAMON-ELSEVIER SCIENCE LTD, 2003. - Vol. 31: Meeting of F4 1 Session of the 34th Scientific Assembly of COSPAR (OCT, 2002, HOUSTON, TEXAS), Is. 7. - P. 1675-1682, DOI 10.1016/S0273-1177(03)00107-8. - Cited References: 4 . - ISBN 0273-1177
РУБ Engineering, Aerospace + Astronomy & Astrophysics + Ecology + Geosciences, Multidisciplinary + Meteorology & Atmospheric Sciences

Аннотация: The term Closed Ecological System (CES) is in wide use. However there is no generally accepted measure of the closure of ecological systems. In order to obtain reproducibility of experiments with natural and man-made CES (with respect to degree of closure) some universal estimate needs to be developed. Understanding ecological systems as a network and closure as the degree of matter recycling allows the use of matrix graphs. Graphs are very natural forms for the presentation of the network of matter flows in ecosystems. An estimate equal to the sum of products of weights of oriented edges that constitute contour is suggested as a measure of the degree of closure in ecosystems. It is shown that this estimate can be uniformly applied to ecosystems of arbitrary size and configuration of flows. (C) 2003 COSPAR. Published by Elsevier Science Ltd. All rights reserved.

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Держатели документа:
Russian Acad Sci, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Bartsev, S.I.; Nelson, M \ed.\; Pechurkin, NS \ed.\; Dempster, WF \ed.\; Somova, LA \ed.\; Somo, , LA \ed.\

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18.


   
    Hydrogen-bond networks between the C-terminus and Arg from the first alpha-helix stabilize photoprotein molecules [Text] / E. V. Eremeeva [et al.] // Photochem. Photobiol. Sci. - 2014. - Vol. 13, Is. 3. - P541-547, DOI 10.1039/c3pp50369k. - Cited References: 22. - The work was supported by RFBR grant 12-04-00753-a, by the Program of the Government of Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.0058). . - ISSN 1474-905X. - ISSN 1474-9092
РУБ Biochemistry & Molecular Biology + Biophysics + Chemistry, Physical
Рубрики:
GREEN FLUORESCENT PROTEIN
   CA2+-REGULATED PHOTOPROTEIN

   BIOLUMINESCENT IMMUNOASSAY

   COELENTERAZINE BINDING

   ANGSTROM RESOLUTION

   ENERGY-TRANSFER

   FUSION PROTEIN

   APO-OBELIN

   AEQUORIN

   EXPRESSION

Аннотация: Previous studies have stated that aequorin loses most of its bioluminescence activity upon modification of the C-terminus, thus limiting the production of photoprotein fusion proteins at its N-terminus. In the present work, we investigate the importance of the C-terminal proline and the hydrogen bonds it forms for photoprotein active complex formation, stability and functional activity. According to the crystal structures of obelin and aequorin, two Ca2+-regulated photoproteins, the carboxyl group of the C-terminal Pro forms two hydrogen bonds with the side chain of Arg21 (Arg15 in aequorin case) situated in the first a-helix. Whereas, deletion or substitution of the C-terminal proline could noticeably change the bioluminescence activity, stability or the yield of an active photoprotein complex. Therefore, modifications of the first alpha-helix Arg has a clear destructive effect on the main photoprotein properties. A C-terminal hydrogen-bond network is proposed to be important for the stability of photoprotein molecules towards external disturbances, when taking part in the formation of locked protein conformations and isolation of coelenterazine-binding cavities.

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Держатели документа:
[Eremeeva, Elena V.
Burakova, Ludmila P.
Krasitskaya, Vasilisa V.
Kudryavtsev, Alexander N.
Frank, Ludmila A.] Russian Acad Sci, Inst Biophys, Siberian Branch, Photobiol Lab, Krasnoyarsk 660036, Russia
[Eremeeva, Elena V.
Burakova, Ludmila P.
Krasitskaya, Vasilisa V.
Kudryavtsev, Alexander N.
Shimomura, Osamu
Frank, Ludmila A.] Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Lab Bioluminescence Biotechnol, Krasnoyarsk 660041, Russia
[Shimomura, Osamu] Marine Biol Lab, Woods Hole, MA 02543 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Eremeeva, E.V.; Burakova, L.P.; Krasitskaya, V.V.; Kudryavtsev, A.N.; Shimomura, O...; Frank, L.A.; RFBR [12-04-00753-a]; Government of Russian Federation [11.G34.31.0058]

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19.


   
    Hydrogen bond network near OH group of 6-(p-hydroxyphenyl) substituent of coelenterazine determines the bioluminescence spectra differences among hydromedusan calcium-regulated photoproteins / E. Vysotski [et al.] // FEBS Open Bio. - 2018. - Vol. 8. - P435-436. - Cited References:0. - This work was supported by RFBR grant 17-04-00764 and a China-Russia international collaboration grant from the Chinese Academy of Sciences and the Natural Science Foundation of China. . - ISSN 2211-5463
РУБ Biochemistry & Molecular Biology


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Держатели документа:
Krasnoyarsk Sci Ctr SB RAS, Fed Res Ctr, Photobiol Lab, Inst Biophys SB RAS, Krasnoyarsk, Russia.
ShanghaiTech Univ, IHuman Inst, Shanghai, Peoples R China.
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA.
Доп.точки доступа:
Vysotski, E.; Markova, S.; Natashin, P.; Stepanyuk, G.; Lee, J.; Malikova, N.; Liu, Z.; RFBR [17-04-00764]; China-Russia international collaboration grant from Chinese Academy of Sciences; Natural Science Foundation of China

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20.


   
    High-resolution structures of scytalone dehydratase-inhibitor complexes crystallized at physiological pH [Text] / Z. . Wawrzak [et al.] // Proteins. - 1999. - Vol. 35, Is. 4. - P. 425-439, DOI 10.1002/(SICI)1097-0134(19990601)35:4425::AID-PROT63.0.CO;2-1. - Cited References: 33 . - ISSN 0887-3585
РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
MAGNAPORTHE-GRISEA
   HEMAGGLUTININ

   GLYCOPROTEIN

   REFINEMENT

   MELANIN

   DISEASE

   SITE

Кл.слова (ненормированные):
structure-based design -- enzyme inhibitors -- X-ray crystallography -- fungicides -- melanin biosynthesis
Аннотация: Scytalone dehydratase is a molecular target of inhibitor design efforts aimed at preventing the fungal disease caused by Magnaporthe grisea. A method for cocrystallization of enzyme with inhibitors at neutral pH has produced several crystal structures of enzyme-inhibitor complexes at resolutions ranging from 1.5 to 2.2 Angstrom Four high resolution structures of different enzyme-inhibitor complexes are described. In contrast to the original X-ray structure of the enzyme, the four new structures have well-defined electron density for the loop region comprising residues 115-119 and a different conformation between residues 154 and 160. The structure of the enzyme complex with an aminoquinazoline inhibitor showed that the inhibitor is in a position to form a hydrogen bond with the amide of the Asn131 side chain and with two water molecules in a fashion similar to the salicylamide inhibitor in the original structure, thus confirming design principles. The aminoquinazoline structure also allows for a more confident assignment of donors and accepters in the hydrogen bonding network, The structures of the enzyme complexes with two dichlorocyclopropane carboxamide inhibitors showed the two chlorine atoms nearly in plane with the amide side chain of Asn131. The positions of Phe53 and Phe158 are significantly altered in the new structures in comparison to the two structures obtained from crystals grown at acidic pH, The multiple structures help define the mobility of active site amino acids critical for catalysis and inhibitor binding. Proteins 1999;35:425-439. (C) 1999 Wiley-Liss, Inc.

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Держатели документа:
Dupont Co, Stine Haskell Res Ctr, Agr Prod, Newark, DE 19714 USA
Dupont Co, Expt Stn, Life Sci, Wilmington, DE USA
Karolinska Inst, Dept Med Biochem & Biophys, Stockholm, Sweden
Russian Acad Sci, Inst Biophys, Krasnoyarsk, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Wawrzak, Z...; Sandalova, T...; Steffens, J.J.; Basarab, G.S.; Lundqvist, T...; Lindqvist, Y...; Jordan, D.B.

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