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Каталог книг и продолжающихся изданий библиотеки Института биофизики СО РАН

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Каталог книг и продолжающихся изданий библиотеки Института биофизики СО РАН (2)

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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Xu, Shicai, Wang, Tiejun, Liu, Guofeng, Cao, Zanxia, Frank, Ludmila A., Jiang, Shouzhen, Zhang, Chao, Li, Zhenhua, Krasitskaya, Vasilisa V., Li, Qiang, Sha, Yujie, Zhang, Xiumei, Liu, Huilan, Wang, Jihua
Заглавие : Analysis of interactions between proteins and small-molecule drugs by a biosensor based on a graphene field-effect transistor
Колич.характеристики :9 с
Коллективы : Taishan Scholars Program of Shandong Province [tsqn201812104]; Qingchuang Science and Technology Plan of Shandong Province [2019KJJ017, 2020KJC004]; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [61671107, 62071085, 11704059, 31802309]; Youth Innovation Team Lead-Education Project of Shandong Educational Committee
Место публикации : Sens. Actuator B-Chem.: ELSEVIER SCIENCE SA, 2021. - Vol. 326. - Ст.128991. - ISSN 0925-4005(eISSN), DOI 10.1016/j.snb.2020.128991
Примечания : Cited References:66. - We are grateful for financial support from the Taishan Scholars Program of Shandong Province (tsqn201812104), the Qingchuang Science and Technology Plan of Shandong Province (2019KJJ017 and 2020KJC004), the National Natural Science Foundation of China (61671107, 62071085, 11704059, and 31802309), and the Youth Innovation Team Lead-Education Project of Shandong Educational Committee.
Предметные рубрики: LABEL-FREE DETECTION
CHEMICAL-VAPOR-DEPOSITION
DNA HYBRIDIZATION
Аннотация: We synthesized large-area single-crystal graphene sheets to use them in biosensors based on field-effect transistors (FET) for quantitative analysis of interaction kinetics and affinity between the imatinib drug and its target protein kinase Abl1. The G-FET biosensor showed an excellent performance and recognized imatinib at as low as 15.5 fM. The biosensor also showed a linear response to the logarithm of imatinib concentration in the 0.1 pM-10 mu M range. This graphene-based FET biosensor (G-FET) was also applied toquantify Abl1 Y253 F mutation and Abl1 dependency on Mg2+ to bind to imatinib in real-time. Results demonstrated in this work clearly showed that the novel G-FET biosensors are very promising to analyze interactions between proteins and low molecular weight drugs.
WOS
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Xu S., Wang T., Liu G., Cao Z., Frank L. A., Jiang S., Zhang C., Li Z., Krasitskaya V. V., Li Q., Sha Y., Zhang X., Liu H., Wang J.
Заглавие : Analysis of interactions between proteins and small-molecule drugs by a biosensor based on a graphene field-effect transistor
Место публикации : Sens Actuators, B Chem: Elsevier B.V., 2021. - Vol. 326. - Ст.128991. - ISSN 09254005 (ISSN), DOI 10.1016/j.snb.2020.128991
Аннотация: We synthesized large-area single-crystal graphene sheets to use them in biosensors based on field-effect transistors (FET) for quantitative analysis of interaction kinetics and affinity between the imatinib drug and its target protein kinase Abl1. The G-FET biosensor showed an excellent performance and recognized imatinib at as low as 15.5 fM. The biosensor also showed a linear response to the logarithm of imatinib concentration in the 0.1 pM-10 ?M range. This graphene-based FET biosensor (G-FET) was also applied to quantify Abl1 Y253 F mutation and Abl1 dependency on Mg2+ to bind to imatinib in real-time. Results demonstrated in this work clearly showed that the novel G-FET biosensors are very promising to analyze interactions between proteins and low molecular weight drugs. © 2020 Elsevier B.V.
Scopus
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Nemtseva, Elena V., Gerasimova, Marina A., Melnik, Tatiana N., Melnik, Bogdan S.
Заглавие : Experimental approach to study the effect of mutations on the protein folding pathway
Колич.характеристики :17 с
Коллективы : Ministry of Science and Education of the Russian Federation [6.7734.2017]; Russian Science Foundation [N14-24-00157]
Место публикации : PLoS One: PUBLIC LIBRARY SCIENCE, 2019. - Vol. 14, Is. 1. - Ст.e0210361. - ISSN 1932-6203, DOI 10.1371/journal.pone.0210361
Примечания : 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.
Предметные 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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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Bolsunovsky A., Frolova T., Dementyev D., Sinitsyna O.
Заглавие : Low doses of gamma-radiation induce SOS response and increase mutation frequency in Escherichia coli and Salmonella typhimurium cells
Место публикации : Ecotoxicol. Environ. Saf.: Academic Press, 2016. - Vol. 134. - С. 233-238. - ISSN 01476513 (ISSN) , DOI 10.1016/j.ecoenv.2016.09.009
Ключевые слова (''Своб.индексиров.''): absorbed dose--ames test--dose rate--mutation rate--sos chromotest--ames test--cell death--dna repair--escherichia coli--experimental model--gamma radiation--limit of detection--long term exposure--mutation rate--nonhuman--sos chromotest--bacteria (microorganisms)--escherichia coli--salmonella typhimurium
Аннотация: This study addresses use of two bacterial test systems (the Ames test and the SOS chromotest) to estimate the effects of low doses of γ-radiation. The most substantial increases in induction of SOS response and mutation frequencies were observed in the first 24 h of exposure to γ-radiation as compared to the cells in the exposure-free control. Gamma-radiation also impaired growth and survival of S. typhimurium cells in the first 24 h. The effects were attenuated at lower exposure doses and at longer exposure times. In the experiments conducted in this study, at 96 h of exposure, the values of some of the γ-radiation effects were lower than the MID (minimum inducing dose) detection limits and, thus, were neglected. Long-term exposure to γ-radiation could also result in combined effects of γ-radiation and the death of cells in the culture. © 2016 Elsevier Inc.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Titushin M.S., Feng Y.G., Stepanyuk G.A., Li Y..., Markova S.V., Golz S..., Wang B.C., Lee J..., Wang J.F., Vysotski E.S., Liu Z.J.
Заглавие : NMR-derived Topology of a GFP-photoprotein Energy Transfer Complex
Колич.характеристики :10 с
Коллективы :
Место публикации : J. Biol. Chem.: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 2010. - Vol. 285, Is. 52. - С. 40891-40900. - ISSN 0021-9258, DOI 10.1074/jbc.M110.133843
Примечания : Cited References: 54. - This work was supported by the National Natural Science Foundation of China, Ministry of Science and Technology of China, CAS Research Grant, CAS Fellowship for Young International Scientists Grant, Russian Foundation for Basic Research (08-09-92209 RFBR-China joint grant), SB RAS Grant 2, "Molecular and Cell Biology" program of RAS, Bayer AG (Germany), and by the University of Georgia Research Foundation and the Georgia Research Alliance.
Предметные рубрики: GREEN-FLUORESCENT PROTEIN
STRUCTURAL DETERMINANTS
RENILLA BIOLUMINESCENCE
ANGSTROM RESOLUTION
CRYSTAL-STRUCTURE
ELECTRON-DENSITY
SOFTWARE
PROGRAM
BINDING
SYSTEM
Аннотация: Forster resonance energy transfer within a protein-protein complex has previously been invoked to explain emission spectral modulation observed in several bioluminescence systems. Here we present a spatial structure of a complex of the Ca2+ regulated photoprotein clytin with its green-fluorescent protein (cgGFP) from the jellyfish Clytia gregaria, and show that it accounts for the bioluminescence properties of this system in vitro. We adopted an indirect approach of combining x-ray crystallography determined structures of the separate proteins, NMR spectroscopy, computational docking, and mutagenesis. Heteronuclear NMR spectroscopy using variously N-15, C-13, H-2-enriched proteins enabled assignment of backbone resonances of more than 94% of the residues of both proteins. In a mixture of the two proteins at millimolar concentrations, complexation was inferred from perturbations of certain H-1-N-15 HSQC-resonances, which could be mapped to those residues involved at the interaction site. A docking computation using HADDOCK was employed constrained by the sites of interaction, to deduce an overall spatial structure of the complex. Contacts within the clytin-cgGFP complex and electrostatic complementarity of interaction surfaces argued for a weak protein-protein complex. A weak affinity was also observed by isothermal titration calorimetry (K-D = 0.9 mM). Mutation of clytin residues located at the interaction site reduced the degree of protein-protein association concomitant with a loss of effectiveness of cgGFP in color-shifting the bioluminescence. It is suggested that this clytin-cgGFP structure corresponds to the transient complex previously postulated to account for the energy transfer effect of GFP in the bioluminescence of aequorin or Renilla luciferase.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Volova T.G., Kozhevnikov I.V., Dolgopolova Yu.B., Trusova M.Yu., Kalacheva G.S., Aref'eva Yu.V.
Заглавие : Physiological and biochemical characteristics and capacity for polyhydroxyalkanoates synthesis in a glucose-utilizing strain of hydrogen-oxidizing bacteria, Ralstonia eutropha B8562
Место публикации : Mikrobiologiya. - 2005. - Vol. 74, Is. 6. - С. 788-794. - ISSN 00263656 (ISSN)
Ключевые слова (''Своб.индексиров.''): glucose-utilizing strain--hydrogen-oxidizing bacteria--polyhydroxyalkanoates--synthesis--bacteria (microorganisms)--cupriavidus necator--bacterial rna--glucose--hydrogen--hydroxybutyric acid--polymer--rna 16s--article--culture medium--genetics--growth, development and aging--metabolism--mutation--oxidation reduction reaction--physiology--wautersia eutropha--culture media--cupriavidus necator--glucose--hydrogen--hydroxybutyrates--mutation--oxidation-reduction--polymers--rna, bacterial--rna, ribosomal, 16s
Аннотация: The physiological, biochemical, genetic, and cultural characteristics of the glucose-utilizing mutant strain Ralstonia eutropha B8562 were investigated in comparison with the parent strain R. eutropha B5786. The morphological, cultural, and biochemical characteristics of strain R. eutropha B8562 were similar to those of strain R. eutropha B5786. Genetic analysis revealed differences between the 16S rRNA gene sequences of these strains. The growth characteristics of the mutant using glucose as the sole carbon and energy source were comparable with those of the parent strain grown on fructose. Strain B8562 was characterized by high yields of polyhydroxyalkanoate (PHA) from different carbon sources (CO 2, fructose, and glucose). In batch culture with glucose under nitrogen limitation, PHA accumulation reached 90% of dry weight. In PHA, ?-hydroxybutyrate was predominant (over 99 mol %); ?-hydroxyvalerate (0.25-0.72 mol %) and ?-hydroxyhexanoate (0.008-1.5 mol %) were present as minor components. The strain has prospects as a PHA producer on glucose-containing media.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Deng L..., Vysotski E.S., Liu Z.J., Markova S.V., Malikova N.P., Lee J..., Rose J..., Wang B.C.
Заглавие : Structural basis for the emission of violet bioluminescence from a W92F obelin mutant
Колич.характеристики :5 с
Место публикации : FEBS Lett.: ELSEVIER SCIENCE BV, 2001. - Vol. 506, Is. 3. - С. 281-285. - ISSN 0014-5793, DOI 10.1016/S0014-5793(01)02937-4
Примечания : Cited References: 15
Предметные рубрики: AEQUORIN
Ключевые слова (''Своб.индексиров.''): calcium-regulated photoprotein--x-ray crystallography--fluorescence--coelenterazine--aequorin
Аннотация: Mutation of the Trp92 that is known to lie within the active site of the photoprotein obelin from Obelia longissima, results in a shift of the bioluminescence color from blue (lambda (max) = 485 nm) to violet. The corrected spectrum shows a new band with lambda (max) = 410 nm now contributing equally to the one at longer wavelength. The crystal structure of this W92F obelin determined at 1.72 Angstrom resolution shows that there is no significant change in the dimensions of the active site between WT obelin (recombinant Ca2+-regulated photoprotein from Obelia longissima) and the mutant. It is proposed that the bioluminescence spectral shift results from removal of a hydrogen bond from the indole of W92 nearby a hydroxyl belonging to the 6-phenyl substituent of the substrate coelenterazine. Propagation of fbis change through a conjugated bond system in the excited state of the product coelenteramide affects the coupling of the N1-position and the hydrogen-bonded Y138. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Brilkov A.V., Loginov I.A., Morozova E.V., Pechurkin N.S.
Заглавие : Trends in microevolution of microbial populations in open systems
Место публикации : Doklady Biochemistry and Biophysics. - 2005. - Vol. 404, Is. 1-6. - С. 349-352. - ISSN 16076729 (ISSN) , DOI 10.1007/s10628-005-0111-x
Ключевые слова (''Своб.индексиров.''): article--bacterial phenomena and functions--bacterium--biological model--culture technique--escherichia coli--evolution--genetics--growth, development and aging--mathematics--methodology--mutation--nanotechnology--ph--physiology--population dynamics--time--bacteria--bacterial physiology--cell culture techniques--escherichia coli--evolution--hydrogen-ion concentration--mathematics--models, biological--mutation--nanotechnology--population dynamics--time factors
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