Библиотека института биофизики СО РАН

Главная

Базы данных

Труды сотрудников ИБФ СО РАН - результаты поиска

Вид поиска

Каталог книг и продолжающихся изданий библиотеки Института биофизики СО РАН

Иностранные журналы библиотеки Института биофизики СО РАН

Отечественные журналы библиотеки Института биофизики СО РАН

Каталог диссертаций ИБФ СО РАН

Труды сотрудников ИБФ СО РАН

Область поиска

Формат представления найденных документов:
полный	информационный	краткий

Отсортировать найденные документы по:
автору	заглавию	году издания	типу документа

Поисковый запрос: (<.>K=Ligands<.>)

Общее количество найденных документов : 5
Показаны документы с 1 по 5

Atomic resolution structure of obelin: soaking with calcium enhances electron density of the second oxygen atom substituted at the C2-position of coelenterazine [Text] / Z. J. Liu [et al.] // Biochem. Biophys. Res. Commun. - 2003. - Vol. 311, Is. 2. - P433-439, DOI 10.1016/j.bbrc.2003.09.231. - Cited References: 29 . - ISSN 0006-291X

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
CRYSTAL-STRUCTURE
   BIOLUMINESCENT PROTEIN
   VIOLET BIOLUMINESCENCE
   PHOTOPROTEIN AEQUORIN
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   W92F OBELIN
   PURIFICATION
   REFINEMENT
   EXPRESSION
Кл.слова (ненормированные):
photoprotein -- bioluminescence -- atomic resolution -- EF-hand
Аннотация: The spatial structure of the Ca2+-regulated photoprotein obelin has been solved to resolution of 1.1 Angstrom. Two oxygen atoms are revealed substituted at the C2-position of the coelenterazine in contrast to the obelin structure at 1.73 Angstrom resolution where one oxygen atom only was disclosed. The electron density of the second oxygen atom was very weak but after exposing the crystals to a trace of Ca2+, the electron densities of both oxygen atoms became equally intense. In addition, one Ca2+ was found bound in the loop of the first EF-hand motif. Four of the ligands were provided by protein residues Asp30, Asn32, Asn34, and the main chain oxygen of Lys36. The other two were from water molecules. From a comparison of B-factors for the residues constituting the active site, it is suggested that the variable electron densities observed in various photoprotein structures could be attributed to different mobilities of the peroxy oxygen atoms. (C) 2003 Elsevier Inc. All rights reserved.

Держатели документа:
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
Univ Georgia, Dept Chem, Athens, GA 30602 USA
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Liu, Z.J.; Vysotski, E.S.; Deng, L...; Lee, J...; Rose, J...; Wang, B.C.

Найти похожие

Ultrafast fluorescence relaxation spectroscopy of 6,7-dimethyl-(8-ribityl)-lumazine and riboflavin, free and bound to antenna proteins from bioluminescent bacteria / V. N. Petushkov [et al.] // Journal of Physical Chemistry B. - 2003. - Vol. 107, Is. 39. - P10934-10939 . - ISSN 1520-6106
Кл.слова (ненормированные):
Bacteria -- Bioluminescence -- Chemical relaxation -- Chromophores -- Dielectric properties -- Proteins -- Solvents -- Bioluminescent bacteria -- Dimethyl ribityl lumazine -- Photobacterium leiognathi -- Riboflavin -- Ultrafast fluorescence relaxation spectroscopy -- Fluorescence
Аннотация: The solvation dynamics of interesting bioluminescent chromophores have been determined, using subpicosecond and wavelength-resolved fluorescence spectroscopy, in combination with global analysis of the multidimensional data sets. The systems investigated comprise the free ligands 6,7-dimethyl-(8-ribityl)-lumazine (lumazine) and riboflavin in an aqueous buffer and both ligands when noncovalently bound to two bacterial bioluminescent antenna proteins: lumazine protein (from Photobacterium leiognathi) and the blue fluorescent protein (from Vibrio fischeri Y1). Fluorescence spectral relaxation of the free ligands is complete within a few picoseconds. Subsequently, the fluorescence intensity increases by ?7% on a time scale of 15-30 ps. Fluorescence spectral relaxation of the protein-bound ligands is largely complete within 1 ps but reveals a small red shift with a minor, but distinctly longer, relaxation time than that of the free ligands, which is tentatively assigned to the relaxation of protein-bound water in the vicinity of the excited chromophore.

Scopus
Держатели документа:
MicroSpectroscopy Centre, Laboratory of Biochemistry, Wageningen University, Dreijenlaan 3, 6703 HA Wageningen, Netherlands
Department of Physics and Astronomy, Faculty of Sciences, Vrije Universiteit, De Boelelaan 1081, 1081 HV Amsterdam, Netherlands
Dept. of Biochem. and Molec. Biology, University of Georgia, Athens, GA 30602, United States
Department of Structural Biology, Faculty of Earth and Life Sciences, Vrije Universiteit, De Boelelaan 1087, 1081 HV Amsterdam, Netherlands
Institute of Biophysics, Academy of Sciences of Russia, Krasnoyarsk 660036, Russian Federation
IPMC, Universite de Lausanne, CH 1015 Lausanne, Switzerland : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Van Stokkum, I.H.M.; Gobets, B.; Van Mourik, F.; Lee, J.; Van Grondelle, R.; Visser, A.J.W.G.

Найти похожие

Properties of recombinant fluorescent proteins from Photobacterium leiognathi and their interaction with luciferase intermediates / V. N. Petushkov, B. G. Gibson, J. Lee // Biochemistry. - 1995. - Vol. 34, Is. 10. - P3300-3309 . - ISSN 0006-2960
Кл.слова (ненормированные):
luciferase -- recombinant protein -- article -- ligand binding -- nonhuman -- priority journal -- protein isolation -- protein protein interaction -- protein stability -- vibrionaceae -- Bacterial Proteins -- Binding Sites -- Carrier Proteins -- Circular Dichroism -- Flavin Mononucleotide -- Fluorescence Polarization -- Genes, Bacterial -- Kinetics -- Ligands -- Luciferase -- Luminescence -- Molecular Sequence Data -- Photobacterium -- Recombinant Proteins -- Spectrophotometry -- Support, U.S. Gov't, P.H.S. -- Photobacterium leiognathi -- Vibrionaceae
Аннотация: Ligand binding and luciferase interaction properties of the recombinant protein corresponding to the lumazine protein gene (EMBL X56534) of Photobacterium leiognathi have been determined by fluorescence dynamics, circular dichroism, gel filtration, and SDS-PAGE. Scatchard analysis of a fluorescence titration shows that the apoprotein possess one binding site, and at 30В°C the KdS (?M) are as follows: 6,7-dimethyl-8-ribityllumazine, 0.26; riboflavin, 0.53; and much more weakly bound FMN, 30. All holoproteins are highly fluorescent and have absorption spectra distinct from each other and from the free ligands. The longest wavelength absorption maxima are, respectively (nm, 2В°C), 420,463, and 458. Ligand binding produces no change in the far-UV circular dichroism; all have mean residual ellipticity at 210 nm of -6500 deg cm2 dmol-1, the same as the native protein. However, in the bioluminescence reaction only the lumazine holoprotein shows a bioluminescence effect. Fluorescence emission anisotropy decay was used to establish that none of these holoproteins complexed with native luciferase and that the lumazine protein alone formed a 1:1 complex with the luciferase hydroxyflavin fluorescent transient and the luciferase peroxyflavin intermediates, revealed by a dominant channel of anisotropy loss, with rotational correlation time of 2.5 ns, and attributed to excitation transfer from the luciferase flavin donor to the acceptor, the lumazine ligand. The complex stability was sufficient to allow its isolation by FPLC gel filtration and verification by SDS-PAGE. These methods also confirmed the absence of interaction of the holoflavoproteins.

Scopus
Держатели документа:
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, United States
Institute of Biophysics, Academy of Sciences of Russia (Siberian Branch), 660036 Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Gibson, B.G.; Lee, J.

Найти похожие

Ultrafast fluorescence relaxation spectroscopy of 6,7-dimethyl-(8-ribityl)-lumazine and riboflavin, free and bound to antenna proteins from bioluminescent bacteria [Text] / V. N. Petushkov [et al.] // J. Phys. Chem. B. - 2003. - Vol. 107, Is. 39. - P. 10934-10939, DOI 10.1021/jp034266e. - Cited References: 52 . - ISSN 1520-6106

РУБ Chemistry, Physical
Рубрики:
TIME-RESOLVED FLUORESCENCE
   VIBRIO-FISCHERI Y1
   FEMTOSECOND SOLVATION DYNAMICS
   FLAVIN ADENINE-DINUCLEOTIDE
   PHOTOBACTERIUM-LEIOGNATHI
   BIOLOGICAL WATER
   SOLVENT DYNAMICS
   DIELECTRIC-RELAXATION
   MOLECULAR-DYNAMICS
   TRYPTOPHAN
Аннотация: The solvation dynamics of interesting bioluminescent chromophores have been determined, using subpicosecond and wavelength-resolved fluorescence spectroscopy, in combination with global analysis of the multidimensional data sets. The systems investigated comprise the free ligands 6,7-dimethyl-(8-ribityl)-lumazine (lumazine) and riboflavin in an aqueous buffer and both ligands when noncovalently bound to two bacterial bioluminescent antenna proteins: lumazine protein (from Photobacterium leiognathi) and the blue fluorescent protein (from Vibrio fischeri Y1). Fluorescence spectral relaxation of the free ligands is complete within a few picoseconds. Subsequently, the fluorescence intensity increases by similar to7% on a time scale of 15-30 ps. Fluorescence spectral relaxation of the protein-bound ligands is largely complete within 1 ps but reveals a small red shift with a minor, but distinctly longer, relaxation time than that of the free ligands, which is tentatively assigned to the relaxation of protein-bound water in the vicinity of the excited chromophore.

WOS
Держатели документа:
Univ Wageningen & Res Ctr, Biochem & Biophys Lab, MicroSpect Ctr, NL-6703 HA Wageningen, Netherlands
Vrije Univ Amsterdam, Fac Sci & Engn, Dept Phys & Astron, NL-1081 HV Amsterdam, Netherlands
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
Vrije Univ Amsterdam, Fac Earth & Life Sci, Dept Biol Struct, NL-1081 HV Amsterdam, Netherlands
Russian Acad Sci, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; van Stokkum, IHM; Gobets, B...; van Mourik, F...; Lee, J...; van Grondelle, R...; Visser, AJWG

Найти похожие

Bioluminescent aptamer-based solid-phase microassay to detect lung tumor cells in plasma / E. E. Bashmakova [et al.] // Talanta. - 2019. - Vol. 199. - P674-678, DOI 10.1016/j.talanta.2019.03.030. - Cited References:19. - The authors are grateful to the staff of Krasnoyarsk regional clinical oncology center named after A.I. Kryzhanovsky and particularly doctor Alexey V. Krat for the experimental material provided. This work was supported by the state budget allocated to the fundamental research at the Russian Academy of Sciences, project No. 0356-2017-0017. . - ISSN 0039-9140. - ISSN 1873-3573

РУБ Chemistry, Analytical
Рубрики:
CONJUGATED NANOPARTICLES
   CANCER
   COLLECTION
   LIGANDS
   PROBES
Кл.слова (ненормированные):
DNA aptamers -- Lung tumor -- Bioluminescent solid-phase microassay
Аннотация: Two high-affinity DNA aptamers for lung tumor cells were applied as biospecific elements in bioluminescent assay of patient blood. The oligonucleotide complementary to the 5' end of both aptamers carrying either biotin or Ca2+-regulated photoprotein obelin was used to form a sandwich-type analytical complex on the surfaces of magnetic streptavidin-activated microspherical particles. Clinical blood samples from cases of morphologically confirmed lung cancer and control samples were analyzed applying the developed assay. From the receiver operator curve (ROC) analysis, the chosen threshold value as clinical decision limit offers the sensitivity of 91.5% and the specificity of 75% (p < 0.001). The area under ROC curve with the value of 0.901 distinguishes well between the two groups under investigation.

WOS,
Смотреть статью,
Scopus
Держатели документа:
RAS, Krasnoyarsk Sci Ctr SB, Fed Res Ctr, Inst Biophys SB, Akademgorodok 50-50, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Svobodny Pr 79, Krasnoyarsk 660041, Russia.
State Med Univ, Partizana Zheleznyaka St 1, Krasnoyarsk 660022, Russia.

Доп.точки доступа:
Bashmakova, Eugenia E.; Krasitskaya, Vasilisa V.; Zamay, Galina S.; Zamay, Tatiana N.; Frank, Ludmila A.; Russian Academy of Sciences [0356-2017-0017]

Найти похожие

Тематический навигатор

Другие библиотеки

Библиотека института физики

Центральная научная библиотека КНЦ СО РАН

Библиотека института химии и химический технологии

Библиотека института вычислительного моделирования

Библиотека института леса

Библиотека СФУ

Краевая научная библиотека

© Международная Ассоциация пользователей и разработчиков электронных библиотек и новых информационных технологий
(Ассоциация ЭБНИТ)