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Relevant bibliographies by topics / Polyhistidine

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Academic literature on the topic 'Polyhistidine'

Author: Grafiati

Published: 28 June 2021

Last updated: 1 February 2022

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Journal articles on the topic "Polyhistidine"

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DePalma, Angelo. "Keeping Tabs on Polyhistidine Tags." Genetic Engineering & Biotechnology News 36, no. 5 (March 2016): 22–24. http://dx.doi.org/10.1089/gen.36.05.12.

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Xu, Zhaohui, and Sang Yup Lee. "Display of Polyhistidine Peptides on theEscherichia coli Cell Surface by Using Outer Membrane Protein C as an Anchoring Motif." Applied and Environmental Microbiology 65, no. 11 (November 1, 1999): 5142–47. http://dx.doi.org/10.1128/aem.65.11.5142-5147.1999.

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ABSTRACT A novel cell surface display system was developed by employingEscherichia coli outer membrane protein C (OmpC) as an anchoring motif. Polyhistidine peptides consisting of up to 162 amino acids could be successfully displayed on the seventh exposed loop of OmpC. Recombinant cells displaying polyhistidine could adsorb up to 32.0 μmol of Cd2+ per g (dry weight) of cells.

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VANGURI, Vijay K., Shuxia WANG, Svetlana GODYNA, Sripriya RANGANATHAN, and Gene LIAU. "Thrombospondin-1 binds to polyhistidine with high affinity and specificity." Biochemical Journal 347, no. 2 (April 10, 2000): 469–73. http://dx.doi.org/10.1042/bj3470469.

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Thrombospondin-1 (TSP1) is a secreted trimeric glycoprotein of 450 kDa with demonstrated effects on cell growth, adhesion and migration. Its complex biological activity is attributed to its ability to bind to cell-surface receptors, growth factors and extracellular-matrix proteins. In this study, we used a 125I solid-phase binding assay to demonstrate that TSP1 binds specifically to proteins containing polyhistidine stretches. Based on studies with three different six-histidine-containing recombinant proteins, we derived an average dissociation constant of 5 nM. The binding of 125I-labelled TSP1 to these proteins was inhibited by peptides containing histidine residues, with the degree of competition being a function of the number of histidines within the peptide. Binding was not inhibited by excess histidine or imidazole, indicating that the imidazole ring is not sufficient for recognition by TSP1. Heparin was a potent inhibitor of binding with a Ki of 50 nM, suggesting that the heparin-binding domain of TSP1 may be involved in this interaction. This was confirmed by the ability of a recombinant heparin-binding domain of TSP1 to directly compete for TSP1 binding to polyhistidine-containing proteins. Affinity chromatography with a polyhistidine-containing peptide immobilized on agarose revealed that TSP1 in platelet releasates is the major polypeptide retained on the six-histidine-peptide column. We conclude that TSP1 contains a high-affinity binding site for polyhistidine and this is likely to be the molecular basis for the observed binding of TSP1 to histidine-rich glycoprotein. The possibility that other polyhistidine-containing proteins also interact with TSP1 warrants further study.

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Putnam, David, Alexander N. Zelikin, Vladimir A. Izumrudov, and Robert Langer. "Polyhistidine–PEG:DNA nanocomposites for gene delivery." Biomaterials 24, no. 24 (November 2003): 4425–33. http://dx.doi.org/10.1016/s0142-9612(03)00341-7.

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Plumptre, Charles D., Abiodun D. Ogunniyi, and James C. Paton. "Polyhistidine triad proteins of pathogenic streptococci." Trends in Microbiology 20, no. 10 (October 2012): 485–93. http://dx.doi.org/10.1016/j.tim.2012.06.004.

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Mateo, Cesar, Gloria Fernandez-Lorente, Benevides C. C. Pessela, Alejandro Vian, Alfonso V. Carrascosa, Jose L. Garcia, Roberto Fernandez-Lafuente, and Jose M. Guisan. "Affinity chromatography of polyhistidine tagged enzymes." Journal of Chromatography A 915, no. 1-2 (April 2001): 97–106. http://dx.doi.org/10.1016/s0021-9673(01)00626-4.

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Tsuji, Shoutaro, Taku Tanaka, Naomi Hirabayashi, Shintaro Kato, Joe Akitomi, Hazuki Egashira, Iwao Waga, and Takashi Ohtsu. "RNA aptamer binding to polyhistidine-tag." Biochemical and Biophysical Research Communications 386, no. 1 (August 2009): 227–31. http://dx.doi.org/10.1016/j.bbrc.2009.06.014.

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Efremenko, Elena, Ilya Lyagin, Yulia Votchitseva, Maria Sirotkina, and Sergey Varfolomeyev. "Polyhistidine-containing organophosphorus hydrolase with outstanding properties." Biocatalysis and Biotransformation 25, no. 1 (January 2007): 103–8. http://dx.doi.org/10.1080/10242420601141796.

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Tang, Quan, Dinglei Zhao, Haiyang Yang, Lijun Wang, and Xingyuan Zhang. "A pH-responsive self-healing hydrogel based on multivalent coordination of Ni2+ with polyhistidine-terminated PEG and IDA-modified oligochitosan." Journal of Materials Chemistry B 7, no. 1 (2019): 30–42. http://dx.doi.org/10.1039/c8tb02360c.

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A multivalent Ni²⁺ coordination hydrogel based on polyhistidine-terminated PEG and IDA-modified oligochitosan with enhanced neutral stability and mild-acid responsiveness is reported herein.

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Miller, Adriana, Dorota Dudek, Sławomir Potocki, Hanna Czapor-Irzabek, Henryk Kozłowski, and Magdalena Rowińska-Żyrek. "Pneumococcal histidine triads – involved not only in Zn2+, but also Ni2+ binding?" Metallomics 10, no. 11 (2018): 1631–37. http://dx.doi.org/10.1039/c8mt00275d.

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Dissertations / Theses on the topic "Polyhistidine"

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Xiao, Xiao Mr. "Purification and Characterization of Rhodobacter sphaeroides Polyhistidine-tagged HemA and Comparison with Purified Polyhistidine-tagged HemT." Bowling Green State University / OhioLINK, 2013. http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1371650467.

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Salichs, Fradera Eulàlia. "Polyhistidine repeats and Dyrk 1a: from the localization on the function." Doctoral thesis, Universitat Pompeu Fabra, 2008. http://hdl.handle.net/10803/7119.

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PolyHistidine repeats and DYRK1A: from the localization to the function
El principal objectiu d'aquesta tesi ha estat el d'esbrinar noves funcions de la proteína quinasa DYRK1A en el nucli cel.lular. Donat que el domini de repetició d'histidines de DYRK1A dirigeix la proteína al compartiment d'speckles nuclears, aquesta propietat ha estat utilitzada per adreçar aquesta pregunta. Els resultats obtinguts en aquesta tesi han permès proposar els homopolímers d'histidina com una nova i general senyal de localització a speckles nuclears. Proteïnes amb segments de polihistidines, la majoria d'elles factors de transcripció, mostren un comportament intranuclear dinàmic, compatible amb un model en el quèl diferents dominis d'interacció competeixen entre ells pel reclutament de la proteína a diferents subcompartiments nuclears. El mecanisme molecular que media l'acumulació a speckles de les proteïnes amb polihistines s'ha estudiat utilitzant DYRK1A com a model. Els resultats obtinguts exclouen la unió a l'RNA com a mecanisme de reclutament i concloure que, aquest, ocorre mitjançant la interacció amb proteïnes residents. S'han identificat dues noves proteïnes interactores per a DYRK1A, l'RNA polimerasa II i el factor de transcripció Brn-3b. La fosforilació de DYRK1A sobre el domini C-terminal o CTD de l'RNA polimerasa II suggereix una funció directa de la quinasa en el procés de transcripció o del seu acoblament al processament d'RNAs missatgers. La fosforilació de DYRK1A sobre el domini d'activació de Brn-3b sembla regular positivament l'activitat transcripcional d'aquest factor. Aquests resultats indiquen una funció activa de DYRK1A en la regulació de la transcripció gènica, tant directament sobre la maquinària transcripcional com indirectament, modulant l'activitat de factors de transcripció.
PolyHistidine repeats and DYRK1A: from the localization to the function
The main objective of this thesis work has been to identify new roles for the protein kinase DYRK1A in the cell nucleus. Given that a histidine repeat in DYRK1A targets the protein to the nuclear speckle compartment, this property has been used as a tool to approach the question. The results obtained in this thesis work have allowed proposing homopolymeric histidine runs as a novel and general nuclear speckle-directing signal. Proteins with polyHistidine segments, mostly transcription factors, present a dynamic intranuclear behaviour compatible with a model in which distinct interacting domains compete for recruiting elements within the nucleus. The molecular mechanisms that mediate speckle accumulation have been studied in DYRK1A as a model system. The results allow excluding RNA binding as the recruiting mechanism and concluding that targeting is mediated by interaction with speckle-resident proteins. Two novel DYRK1A interactors have been identified during the study, the RNA polymerase II and the transcription factor Brn-3b. DYRK1A phosphorylation of the C-terminal domain or CTD of the RNA polymerase II suggests a direct role of DYRK1A on transcription or coupling of transcription with RNA processing. DYRK1A phosphorylation of Brn-3b within its activation domain seems to positively regulate Brn-3b transcriptional activity. These results confirm an active role for DYRK1A in gene transcription regulation both direct on the transcriptional machinery and indirect by modulating the activity of transcription factors.

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Raghunathan, Dhaarini. "Characterisation of the three polyhistidine triad (PHT) proteins of Streptococcus suis." Thesis, University of Cambridge, 2015. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.708655.

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Keith, Sydney R., and Jonathan M. Ph D. Peterson. "Experimental Protocol for the Production of Bacterial Expressed CTRP3." Digital Commons @ East Tennessee State University, 2018. https://dc.etsu.edu/asrf/2018/schedule/182.

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INTRODUCTION: Previous studies have shown that mammalian expressed CTRP3 functions to lower blood glucose levels in transgenic mice. However, the production of mammalian expressed CTRP3 is expensive and can only yield up to 1mg/L of recombinant protein. On the contrary, bacterial expressed CTRP3 is relatively inexpensive and can theoretically produce 70mg of recombinant protein per L of bacteria. The purpose of this experiment is to see if functional CTRP3 protein can be produced effectively and economically using bacterial expression system. METHODS: The ctrp3 gene was inserted into a bacterial expression plasmid vector and transfected into Escherichia Coli (E. coli) bacterium to produce recombinant Polyhistidine-tagged-CTRP3 in the presence of L-Arabinose. Optimal expression parameters were then tested in the transfected bacteria. Optimal expression was confirmed by measurement of CTRP3 in through immunoblotting. RESULTS: Once optimal expression conditions were established, large amounts of CTRP3 were generated and purified by commercial HIS purification systems. Due to post-translation modification of CTRP3, it is unclear if the purified CTRP3 will be functional. The next step in the process is to optimize the purification protocol and test the functionality of the bacterial expressed CTRP3. Support or Funding Information This research was supported in part by National Institute on Alcohol Abuse and Alcoholism of the National Institutes of Health under Award Number R03AA023612 and East Tennessee State University Research Development Committee (E82262).

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Ring, Christine. "Optimization of in vitro transcription/translation conditions for in vitro compartmentalization studies and synthesis of 4-fluorohistidine." VCU Scholars Compass, 2017. http://scholarscompass.vcu.edu/etd/4807.

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Genetic code expansion allows the incorporation of non-canonical amino acids with a variety of new functional groups: fluorescent amino acids,1-3 azides,4-6 alkynes,5-10 and photocrosslinkers.4,11,12 This incorporation requires the evolution of new tRNA/aminoacyl tRNA sythetase pairs. Traditionally screenings of novel tRNA/aminoacyl tRNA synthetase pairs have been done in vivo. While these in vivo screenings have proven robust, they are limited in multiple ways: non-canonical amino acids (ncAAs) must be nontoxic and bioavailable. Furthermore, library size is limited by transformation efficiency. Lastly, in vivo screenings require substantial amounts of the target ncAA, which is often not available in large masses. In vitro screenings bypass these limitations: toxicity and bioavailibilty are no longer concerns. Library size can be expanded by several orders of magnitude as we are no longer limited by transformation efficiency. Lastly, because in vitro transcription/translation reactions are routinely conducted on the μL scale, ncAA usage can be minimized. We set out to use in vitro compartmentalization to further expand the code. In an in vitro compartmentalization screening, the water droplets in a water-in-oil emulsion serve as separate reaction chambers in which individual library members are transcribed and translated. Here we report optimization of S30 transcription/translation reactions. Optimizations include cell lysis method, reaction temperature, template amount, and T7 RNA polymerase amounts. Yields remained low and we transistioned into the use of PURExpress. Fluorohistidines are isosteric with histidine, but not isoelectronic.13 This change in environment results in a reduction of pKa. We set out to synthesize 4-fluorohistidine to use as a pH probe in several target proteins. A synthesis of 4-fluorohistidine was published in 1973.14,15 We were able to improve upon this synthesis by reducing cost and improving yield of a key step in the reaction. Next, small peptides with polyhistidine tags were translated in vitro using our 4-fluorohistidine. We are calling this polyhistidine tag incorporating 4-fluorohistidine our “hexafluorohistag.” Because of the reduced pKa of the 4-fluorohistidine, the hexafluorohistag showed affinity to Nickel-NTA resin even at reduced pH. This allowed for the purification of hexafluorohistagged peptides in the presence of traditional polyhistidine-tagged peptides.

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"Polyhistidine repeats and Dyrk 1a: from the localization on the function." Universitat Pompeu Fabra, 2008. http://www.tesisenxarxa.net/TDX-0305109-143811/.

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Číhařová, Barbora. "Studium účinku modifikace virových částic polyhistidinem na jejich intracelulární lokalizaci a dopravu genů do jádra." Master's thesis, 2021. http://www.nusl.cz/ntk/nusl-446452.

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Viral vectors derived from mouse polyomavirus are a convenient tool for studying the targeted delivery of therapeutical agents into the cells and cellular organelles. Vectors derived from mouse polyomavirus face difficulties similar to other nanoparticles, as they often end up trapped inside an endosome where they are subsequently degraded. This diploma explored the potential of vector modifications, which have the potential to make the transport to the nucleus or cytosol more effective. This work had particularly focused on increasing the transduction efficiency by modifying particle's internally localized VP3 capsid protein with covalently bound membrane-penetrating peptides. Primary covalent genetic modification to the VP3 protein was the polyhistidine peptide KH27K. Its potential of improving the transduction effectivity was compared with two other peptide modifications - LAH4 and R8. The results of the transduction test showed that covalently bound R8 peptide had many-fold improved the transport to the nucleus when compared to the unmodified particles. The modification with LAH4 peptide had been regarded more effective only when was associated with the particles non-covalently. In such scenario the transduction efficiency rose 40-times when compared with unmodified particles. Polyhistidine...

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Russell, Bonnie Leigh. "Expression, solubilisation, purification and characterisation of recombinant bluetongue virus viral protein 7." Diss., 2018. http://hdl.handle.net/10500/24951.

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Bluetongue virus belongs to the Orbivirus genus from the Reoviridae family. It infects predominantly domestic and wild ruminants and is economically significant worldwide. Bluetongue virus VP7 forms the intercepting layer between the outer capsid (VP2 and VP5) and VP3 which surrounds the genomic material. BL21(DE3), NiCo21(DE3), C43(DE3) pLysS and KRX Escherichia coli cells were transformed with a pET28a plasmid with the cDNA sequence encoding Bluetongue virus VP7. Expression of Bluetongue virus VP7 was tested at post induction temperatures between 16˚C and 37 ˚C, at inducer concentrations between 0.1 mM and 1.0 mM isopropyl-β-D-thiogalactopyranoside in BL21(DE3), NiCo21(DE3) and C43(DE3) pLysS cells and 0.05 % and 0.15 % rhamnose for KRX cells, in two types of growth media (LB and 2xYT) and post-induction growth times between two and 16 hours. Under all conditions tested; Bluetongue virus VP7 expression was found to be predominantly in the insoluble fraction (pellet). BL21(DE3) and NiCo21(DE3) cells were chosen and grown for five hours post induction, induced with 0.1 mM isopropyl-β-D-thiogalactopyranoside and grown at a post-induction temperature of 37 ˚C. Bluetongue virus VP7 in bacterial cell inclusion bodies was solubilised using urea and a freeze-thaw step. Solubilisation was tested with urea concentrations between 2 M and 8 M, with solubilisation efficiency not increasing past 5 M urea. Solubilized Bluetongue virus VP7 was purified using nickel-affinity chromatography. Purified Bluetongue virus VP7 was then probed with far-UV circular dichroism and intrinsic fluorescence in several buffer conditions including different urea and guanidinium chloride concentrations as well as in the presence of glycerol and sodium chloride. Guanidinium chloride was able to cause Bluetongue virus VP7 unfolding, and the unfolding transition had 94 % and 89 % reversibility at 218 nm and 222 nm respectively. Bluetongue virus VP7 was shown to contain a native-like structure in 20 % glycerol and in up to 8 M urea and was found to be stable till at least 55 ˚C, even in the presence of 5 M urea. Glycerol and sodium chloride influenced the conformation of the protein resulting in different unfolding transitions. Thermal unfolding of Bluetongue virus VP7 was found to be irreversible.
Life and Consumer Sciences
M. Sc. (Life Sciences)

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Books on the topic "Polyhistidine"

1

Toso, Robert. Expression and partial purification of a polyhistidine-tagged human DNA Topoisomerase II gas fusion protein, in the baculovirus expression system. Ottawa: National Library of Canada, 1993.

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Book chapters on the topic "Polyhistidine"

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Loughran, Sinéad T., Ronan T. Bree, and Dermot Walls. "Purification of Polyhistidine-Tagged Proteins." In Methods in Molecular Biology, 275–303. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-6412-3_14.

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Krause, Katherine D., Hsin-Yun Tsai, Kelly Rees, Hyungki Kim, and W. Russ Algar. "Preparation and Characterization of Quantum Dot-Peptide Conjugates Based on Polyhistidine Tags." In Methods in Molecular Biology, 175–218. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1617-8_16.

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de Costa, Fernanda, Carla J. S. Barber, Pareshkumar T. Pujara, Darwin W. Reed, and Patrick S. Covello. "Purification of a Recombinant Polyhistidine-Tagged Glucosyltransferase Using Immobilized Metal-Affinity Chromatography (IMAC)." In Methods in Molecular Biology, 91–97. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3393-8_9.

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Bornhorst, Joshua A., and Joseph J. Falke. "[16] Purification of proteins using polyhistidine affinity tags." In Methods in Enzymology, 245–54. Elsevier, 2000. http://dx.doi.org/10.1016/s0076-6879(00)26058-8.

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Takeda, Takumi. "Polyhistidine Affinity Chromatography for Purification and Biochemical Analysis of Fungal Cell Wall-Degrading Enzymes." In Affinity Chromatography. InTech, 2012. http://dx.doi.org/10.5772/36411.

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