Academic literature on the topic 'Tyrosine fluorescence'
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Journal articles on the topic "Tyrosine fluorescence"
Turner, R. J., R. S. Roche, R. S. Mani, and C. M. Kay. "Tyrosine and tyrosinate fluorescence of S-100b. A time-resolved nanosecond fluorescence study. The effect of pH, Ca(II), and Zn(II)." Biochemistry and Cell Biology 67, no. 4-5 (April 1, 1989): 179–86. http://dx.doi.org/10.1139/o89-028.
Full textO'Neil, J. D. J., and T. Hofmann. "Tyrosine and tyrosinate fluorescence of pig intestinal Ca2+-binding protein." Biochemical Journal 243, no. 2 (April 15, 1987): 611–15. http://dx.doi.org/10.1042/bj2430611.
Full textShen, Yiming, Deyi Zhu, Wenhui Lu, Bing Liu, Yanchun Li, and Shan Cao. "The Characteristics of Intrinsic Fluorescence of Type I Collagen Influenced by Collagenase I." Applied Sciences 8, no. 10 (October 16, 2018): 1947. http://dx.doi.org/10.3390/app8101947.
Full textGahn, L. G., and R. Roskoski. "Tyrosine hydroxylase activity and extrinsic fluorescence changes produced by polyanions." Biochemical Journal 295, no. 1 (October 1, 1993): 189–94. http://dx.doi.org/10.1042/bj2950189.
Full textWillis, K. J., and A. G. Szabo. "Fluorescence decay kinetics of tyrosinate and tyrosine hydrogen-bonded complexes." Journal of Physical Chemistry 95, no. 4 (February 1991): 1585–89. http://dx.doi.org/10.1021/j100157a015.
Full textJiang, Chao, Ya Li, Chenghui Liu, Liying Qiu, and Zhengping Li. "A general and versatile fluorescence turn-on assay for detecting the activity of protein tyrosine kinases based on phosphorylation-inhibited tyrosyl oxidation." Chemical Communications 52, no. 85 (2016): 12570–73. http://dx.doi.org/10.1039/c6cc07035c.
Full textWANG, Jing-Dong, Shuang LI, Rong LÜ, and An-Chi YU. "Fluorescence Quenching of Eosin Y by Tyrosine." Acta Physico-Chimica Sinica 31, no. 9 (2015): 1787–94. http://dx.doi.org/10.3866/pku.whxb201507241.
Full textSeethala, Ramakrishna. "Fluorescence Polarization Competition Immunoassay for Tyrosine Kinases." Methods 22, no. 1 (September 2000): 61–70. http://dx.doi.org/10.1006/meth.2000.1037.
Full textGavrilov, V. B., A. V. Lychkovskii, E. P. Shostak, and S. V. Konev. "Fluorescence assay of tyrosine in blood plasma." Journal of Applied Spectroscopy 65, no. 3 (May 1998): 379–84. http://dx.doi.org/10.1007/bf02675456.
Full textTominaga, Tania Toyomi, Hidetake Imasato, Otaciro Rangel Nascimento, and Marcel Tabak. "Interaction of tyrosine and tyrosine dipeptides with Cu2+ ions: A fluorescence study." Analytica Chimica Acta 315, no. 1-2 (October 1995): 217–24. http://dx.doi.org/10.1016/0003-2670(95)00303-h.
Full textDissertations / Theses on the topic "Tyrosine fluorescence"
Reynolds, Andrew Robert. "Functional fluorescence imaging of receptor tyrosine kinase activity in cells." Thesis, University College London (University of London), 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.398898.
Full textLee, Jinkeun. "Studies of the fluorescence of Tyrosine and Tryptophan using trilinear analysis /." The Ohio State University, 1994. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487859879938668.
Full textKIM, SOYEON. "INVESTIGATING THE MOLECULAR INTERACTION OF ERBB RECEPTOR TYROSINE KINASES USING FLUORESCENCE CROSS CORRELATION SPECTROSCOPY." University of Akron / OhioLINK, 2021. http://rave.ohiolink.edu/etdc/view?acc_num=akron1632756640189756.
Full textSuen, Fung Ki. "Tyrosine hydroxylase-green fluorescence protein transgenic zebrafish as a biosensor and animal model for nicotine and ketamine drug effects." HKBU Institutional Repository, 2012. https://repository.hkbu.edu.hk/etd_ra/1449.
Full textPaul, Uchenna Prince. "Fluorescence Detectors for Proteins and Toxic Heavy Metals." Diss., CLICK HERE for online access, 2004. http://contentdm.lib.byu.edu/ETD/image/etd416.pdf.
Full textVasconcelos, Stanley Nunes Siqueira. "Tirosina, substrato em reações de acoplamento cruzado: síntese de dipeptídeos Tyr-Tyr, heterociclos e investigação da atividade biollógica contra células cancerígenas e parasitárias." Universidade de São Paulo, 2017. http://www.teses.usp.br/teses/disponiveis/9/9138/tde-20122017-144457/.
Full textTyrosine, a proteinogenic amino acid of fundamental importance for life, was the object of study for the research that is presented in this thesis. When 3-iodotyrosine was used in the three different types of cross-coupling reactions that have been exploited the most in recent years, namely the Suzuki-Miyaura, Heck and Sonogashira coupling reactions, 3-iodotyrosine as an excellent substrate for the formation of biaryl units, stilbene derivatives, 1,2,3-triazoletype heterocycles, quinolines, benzofurans and flavones, and Tyr-Tyr dipeptides. This work is organized into sections in order to facilitate ease of reading. The reaction between 3-iodotyrosine and different boron nucleophiles via the Suzuki- Miyaura coupling reaction, in addition to giving the biaryl units, also provided stilbene derivatives, which were used as substrates for the construction of quinolines via multicomponent Povarov reactions. The Povarov was performed with silver catalysis under 40 minutes of microwave irradiation. Some of these stilbene derivatives showed a marked fluorescence, which was measured in solvents with different polarities. By exploring the Sonogashira coupling reaction between 3-iodotyrosine and acetylenes, alkynyl derivatives could be conveniently prepared, which in turn could be used as starting materials in Huisgen cycloaddition reactions to synthesize1,2,3-triazole rings. Products from the stereoselective addition of oxa-Michael, between the phenolic ring of tyrosine and propargyl aldehydes, provided 945;,946;-unsaturated carbonyl compounds capable of reacting via Heck intramolecular coupling, leading to 2-aryl-3-formyl-5-alanylbenzofurans or by simply changing the inert atmosphere of nitrogen by carbon monoxide, the formation of 2- aryl-6-alanylflavones via reductive intramolecular acylation. In addition to the synthesis methodology explored in the thesis, some of the compounds showed selective biological activity against melanoma and leukemia cells, as well as antiparasitic activity against Plasmodium falciparum, without affecting the proliferation of healthy cells. In this way, the presented results add even more synthetic and biological value to the amino acid tyrosine, explored in an unprecedented way.
Nag, Lipsa. "Internal dynamics of flavoproteins studied by femtosecond spectroscopy." Thesis, Université Paris-Saclay (ComUE), 2018. http://www.theses.fr/2018SACLX121/document.
Full textNature employs charge transfer reactions in many biological functions. Redox-active cofactors like flavins (FAD and FMN) are often implicated in such reactions. Charge transfer in proteins often proceeds via formation of radical intermediates. The amino acid radicals of tyrosine (TyrOH) and tryptophan are thought to play important roles as intermediates in intra- and interprotein charge transfer reactions. Tryptophanyl radicals (both protonated cation and deprotonated neutral forms), had been characterized before. However, tyrosyl radicals had only been characterized in the neutral form, and were thought to be formed by concerted electron extraction and deprotonation of tyrosine. Short-lived intermediates are often difficult to observe in biochemical reactions, but may be populated when they can be photochemically formed using short light pulses.In this work, we have characterized intermediates in non-functional charge transfer reactions in flavoproteins using femtosecond time-resolved fluorescence and absorption spectroscopy. Excited states and product states formed in the wild type and mutant forms of the methyltransferase flavoenzyme TrmFO from Thermus thermophilus were investigated. In the TrmFO active site, a tyrosine (Tyr343), is closely stacked on the FAD isoalloxazine ring and a cysteine (Cys51) can form a highly fluorescent adduct with the FAD. In the mutant C51A, FADox fluorescence is strongly quenched by electron transfer from the Tyr343 in ~1ps. The resulting product state displayed a distinct spectral feature- a strong absorption band at ~490 nm unlike any previously characterized radical species. It was assigned to the radical cation of tyrosine (TyrOH•+) which had never been observed before. The FAD•-TyrOH•+ intermediate, is very short-lived as it decays in ~3ps, through charge recombination. As a general conclusion, despite the very low pKa of TyrOH•+, electron transfer from tyrosine can occur without concomitant proton transfer.Using polarization photoselection experiments, we estimated the dipole moment direction for this new transition. The resultant angle between the excited FADox transition and the probed TyrOH•+ transition in C51A TrmFO was 31º±5º. This result sets the orientation of the dipole moment of the transition in the molecular frame of the phenol ring. The finding of distinct directions for the excited FAD transition band and the 490 nm transition confirms their origin in different molecular entities.Following the results from TrmFO, we reinvestigated the photochemistry in the model flavoprotein glucose oxidase (GOX). Here, both tryptophan and tyrosine residues are located in the vicinity of FAD and the photoproduct evolution on the picosecond timescale is more complex. Distinct phases of excited state decay with time constants of 1ps and ~4ps were observed, as well as phases of ~4ps, ~37 ps and a longer-lives phase for product state evolution. Consequently, a comprehensive model for the involvement of radicals of tyrosine and tryptophan and, the different FAD redox states, in the light-induced charge separation and recombination in GOX was made. Partial involvement of the TyrOH•+ radical cation, spectrally similar to C51A TrmFO, was required for the 4 ps and 37 ps phases to account for the ensemble of data. This result explains previous enigmatic features and indicates the involvement of TyrOH•+ in a variety of protein systems.So far, only the deprotonated tyrosyl radical TyrO• had been observed as a functional intermediate in several systems. The visualization of protonated TyrOH•+ radical in TrmFO C51A and GOX suggests the possibility of its intermediate formation as a precursor of TyrO• in functional biochemical reactions.Finally, in TrmFO the construction of specific variants with site-directed mutagenesis was initiated to study active-site flexibility using electron transfer rates as conformational markers. Further experimental and modeling work is required to pursue this goal
Peyressatre, Marion. "Développement de biosenseurs fluorescents et d’inhibiteurs pour suivre et cibler CDK5/p25 dans le glioblastome." Thesis, Montpellier, 2016. http://www.theses.fr/2016MONT3513/document.
Full textCDK5 is a protein kinase ubiquitously expressed but mainly activated in the central nervous system, where it plays an important role in neuronal functions such as synaptic transmission, axonal guidance and migration, synaptic plasticity and neuronal development. CDK5 is associated with p35 protein at the cell membrane, then activated by calpain-mediated cleavage of p35 into p25, which promotes relocalization of CDK5/p25 into the cytoplasm. CDK5/p25 phosphorylates a wide variety of substrates including Tau, thereby contributing to appearance of neurofibrillary plaques responsable for neurodegenerative pathologies such as comme Alzheimer’s et Parkinson’s, when hyperactivated. More recent studies suggest that CDK5 expression and hyperactivation are involved in glioblastoma during cell invasion and CDK5 expression has been reported to be correlated with the pathological grade of gliomas. However there are currently no tools available to monitor CDK5/p25 activity in its native cellular environment, in tissues or in tumours, due to an overall lack of reliable tools to quantify dynamic changes in its kinase activity in a sensitive and continuous fashion. Furthermore, few inhibitors are currently available to target CDK5/p25 in a specific fashion and most of them are ATP competitive inhibitors.The first goal of my thesis was to develop a fluorescent peptide biosensor named CDKACT5, that specifically reports on recombinant CDK5/p25 and on endogenous CDK5 activity in cell extracts in a dynamic and reversible fashion following stimulation or inhibition of this kinase. Once validated in vitro, this biosensor was applied to detect alterations in CDK5/p25 activity in different glioblastoma cell lines in fluorescent kinase activity assays. Finally CDKACT5 was introduced into cultured neuronal cells to monitor dynamic changes in CDK5/p25 activity by fluorescence imaging and time-lapse microscopy.The second goal of my thesis project consisted in developing a conformational fluorescent biosensor to identify non-ATP competitive inhibitors targeting the activation loop of CDK5. CDKCONF5 was implemented to perform a high throughput screen of three small molecule libraries. The hits identified were validated and characterized to determine their inhibitory potential in kinase activity and proliferation assays, as well as their mechanism of action. These compounds constitute promising for selective chemotherapy in glioblastoma
Galvan, Barbara. "Part I, highly sensitive hybridization assays for prostate-specific antigen mRNA based on time-resolved fluorescence and bioluminescence, Part II, fluorometric and time-resolved immunofluorometric assays for protein-tyrosine phosphatase and kinase activity." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1996. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/NQ30283.pdf.
Full textMatôzo, Huita do Couto. "Estudos estruturais do domínio catalítico da proteína tirosina fosfatase eta de rato." Universidade de São Paulo, 2008. http://www.teses.usp.br/teses/disponiveis/76/76132/tde-16012009-042410/.
Full textThe rat protein tyrosine phosphatase eta, rPTPeta, is a transmembrane RPTP, with an intracellular portion composed of a unique catalytic region. The rPTPeta and the human homolog DEP-1 are down-regulated in rat and human neoplastic cells, respectively. However, the malignant phenotype is reverted after exogenous reconstitution of rPTPeta, suggesting that its function restoration could be an important tool for gene therapy of several types of cancer. Therefore, the objective of our project aimed on the molecular, biophysical and structural study of the catalytic domain of rPTPeta, rPTPetaDC. We began our study cloning the rPTPetaDC into PET28a(+) vector, followed by its expression in Escherichia coli, and purification. The His6-tag from the rPTPetaDC purified was subsequently removed by thrombin digestion. PhastGel IEF electrophoresis demonstrated that the isoelectric point of the 41kDa was 7.3. To assess the functionality of the rPTPetaDC we used the pNPP hydrolysis assay and observed that the enzyme has a specific activity of 9nmol/min/ug. The experimentally determined rPTPetaDC specific activity showed to be in the same range as the previously reported activities for RPTPu, RPTPalfa, PTPB1 and SHP2. The secondary structure and stability of the recombinant protein was analyzed by circular dichroism and fluorescence spectroscopy. The results demonstrated that rPTPetaDC was stable at 18 Celsius and properly folded (Santos, et al., Prot. Expr. Purif., 2005. In attachment A). Then, the purified protein was submitted to different crystallization conditions and structural studies in solution. Crystals appeared at 0.1M MES, pH 6.5 and 20% PEG 10,000 and diffracted with resolution of 1.87Å. The crystals belong to spatial group P2(1)2(1)2(1) with unit cell parameters of a=46.46, b=63.07, c=111.64Å and contained one molecule for asymmetric unit (Matozo, et al., Acta crystallog. F, 2006. In attachment B). Also, the structural of rPTPetaDC, in solution, was analyzed by SAXS and fluorescence anisotropy. SAXS data showed that the protein forms elongated dimers in solution with an Rg of 2.65nm and a Dmax of 8.5nm. The rPTPetaDC conformation in solution, studied by homology models, suggested that the rPTPetaDC dimer architecture is more closely related to the crystal structure of RPTPalfa-D1. The characterization of rPTPetaDC by fluorescence anisotropy measurements demonstrated that the Kd of the dimer is 21.6 + 2.0uM and the energy Gibbs dimer-monomer is equal to 7.2kcal/mol (Matozo, et al., Bioph. J., 2007. In attachment C).
Books on the topic "Tyrosine fluorescence"
Nowak-Thompson, Brian. Biosynthetic studies on the chromophore of pseudobactin from Pseudomonas fluorescens B10. 1993.
Find full textBook chapters on the topic "Tyrosine fluorescence"
Vekshin, Nikolai L. "Division of Tyrosine and Tryptophan Fluorescence Components." In Photonics of Biopolymers, 56–61. Berlin, Heidelberg: Springer Berlin Heidelberg, 2002. http://dx.doi.org/10.1007/978-3-662-04947-1_7.
Full textSchumacher, Dominik, Heinrich Leonhardt, Christian P. R. Hackenberger, and Jonas Helma. "One-Step Fluorescent Protein Labeling by Tubulin Tyrosine Ligase." In Methods in Molecular Biology, 167–89. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9654-4_12.
Full textHofmann, Roseanne M., Graham J. Cotton, William Bornman, Emmanual Chang, and Tom W. Muir. "Fluorescent Biosensor for CrkII Phosphorylation by the Abl Tyrosine Kinase." In Peptides: The Wave of the Future, 992–93. Dordrecht: Springer Netherlands, 2001. http://dx.doi.org/10.1007/978-94-010-0464-0_463.
Full textBerkel, Willem J. H. van, Edwin J. Bakx, Franz Miiller, Wicher J. Weyer, Peter A. Jekel, Jaap J. Beintema, Herman A. Schreuder, et al. "Chemical modification of tyrosine-38 in j>.-hydroxybenzoate hydroxylase from Pseudomonas fluorescens by 5'-Pfluorosulfonylbenzoyladenosine: A probe for the elucidation of the NADPH binding site?" In Flavins and Flavoproteins 1987, edited by D. E. Edmondson and D. B. McCormick, 549–52. Berlin, Boston: De Gruyter, 1987. http://dx.doi.org/10.1515/9783110884715-092.
Full textConference papers on the topic "Tyrosine fluorescence"
Yang, Hui, Xue Xiao, Xuesong Zhao, and Yan Wu. "Intrinsic Fluorescence Spectra of Tryptophan, Tyrosine and Phenyloalanine." In 5th International Conference on Advanced Design and Manufacturing Engineering. Paris, France: Atlantis Press, 2015. http://dx.doi.org/10.2991/icadme-15.2015.46.
Full textYang, Hui, Xue Xiao, Xuesong Zhao, and Yan Wu. "Intrinsic fluorescence spectra of tryptophan, tyrosine and phenyloalanine." In Selected Papers of the Chinese Society for Optical Engineering Conferences held October and November 2016, edited by Yueguang Lv, Jialing Le, Hesheng Chen, Jianyu Wang, and Jianda Shao. SPIE, 2017. http://dx.doi.org/10.1117/12.2268397.
Full textVarghese, Jeena, Subin Thomas, and C. Sudarsanakumar. "L-Tyrosine functionalized ZnO for the fluorescence detection of phenol." In THE 3RD INTERNATIONAL CONFERENCE ON OPTOELECTRONIC AND NANO MATERIALS FOR ADVANCED TECHNOLOGY (icONMAT 2019). Author(s), 2019. http://dx.doi.org/10.1063/1.5093886.
Full textSanyal, Gautam, Faith Thompson, and David Puett. "Fluorescence spectroscopic studies of tyrosine environment and ligand binding of plant calmodulin." In OE/LASE '90, 14-19 Jan., Los Angeles, CA, edited by Joseph R. Lakowicz. SPIE, 1990. http://dx.doi.org/10.1117/12.17754.
Full textSingh, Amit T., and M. M. Khandpekar. "Upconversion fluorescence tyrosine doped LaF3:Dy quantum dots useful in biolabeling and biotagging." In DAE SOLID STATE PHYSICS SYMPOSIUM 2017. Author(s), 2018. http://dx.doi.org/10.1063/1.5028665.
Full textBrown, David W., Louis J. Libertini, and Enoch W. Small. "Using the decay of intrinsic tyrosine fluorescence of core particles to monitor conformational changes." In OE/LASE '92, edited by Joseph R. Lakowicz. SPIE, 1992. http://dx.doi.org/10.1117/12.58277.
Full textLakowicz, Joseph R., Gabor Laczko, Ignacy Gryczynski, Henryk Cherek, Stephen N. Joffe, and John A. Parrish. "A 2 GHz Frequency-Domain Fluorometer; Picosecond Resolution Of Tyrosine Fluorescence And Anisotropy Decays." In Cambridge Symposium-Fiber/LASE '86. SPIE, 1987. http://dx.doi.org/10.1117/12.937326.
Full textZhdanova, Nadezda, Evgeny Shirshin, Victor Fadeev, and Alexander Priezzhev. "SDS-binding assay based on tyrosine fluorescence as a tool to determine binding properties of human serum albumin in blood plasma." In Saratov Fall Meeting 2015, edited by Elina A. Genina, Valery V. Tuchin, Vladimir L. Derbov, Dmitry E. Postnov, Igor V. Meglinski, Kirill V. Larin, and Alexander B. Pravdin. SPIE, 2016. http://dx.doi.org/10.1117/12.2229850.
Full textZhdanova, N. G., E. A. Shirshin, I. M. Panhishin, and V. V. Fadeev. "Study of Tyrosine to Tryptophan Energy Transfer in Human Serum Albumin in Presence of Surfactant via Steady-State, Nonlinear and Time-Resolved Fluorescence Techniques." In Frontiers in Optics. Washington, D.C.: OSA, 2013. http://dx.doi.org/10.1364/fio.2013.ftu1d.4.
Full textAsami, Tokiko, Wataru Kawahata, and Masaaki Sawa. "Abstract C94: A novel binding assay to identify inhibitors that bind to inactive forms of Bruton's tyrosine kinase based on fluorescence resonance energy transfer." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Nov 12-16, 2011; San Francisco, CA. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1535-7163.targ-11-c94.
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