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Relevant bibliographies by topics / Guanidine hydrochloride; Denaturants

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Academic literature on the topic 'Guanidine hydrochloride; Denaturants'

Author: Grafiati

Published: 4 June 2021

Last updated: 15 February 2022

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Journal articles on the topic "Guanidine hydrochloride; Denaturants"

1

Stepanenko, Olesya, Olga Stepanenko, Irina Kuznetsova, and Konstantin Turoverov. "The Pathways of the iRFP713 Unfolding Induced by Different Denaturants." International Journal of Molecular Sciences 19, no. 9 (2018): 2776. http://dx.doi.org/10.3390/ijms19092776.

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Near-infrared fluorescent proteins (NIR FPs) based on the complexes of bacterial phytochromes with their natural biliverdin chromophore are widely used as genetically encoded optical probes for visualization of cellular processes and deep-tissue imaging of cells and organs in living animals. In this work, we show that the steady-state and kinetic dependencies of the various spectral characteristics of iRFP713, developed from the bacterial phytochrome RpBphP2 and recorded at protein unfolding induced by guanidine hydrochloride (GdnHCl), guanidine thiocyanate (GTC), and urea, differ substantiall

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2

West, S. M., A. D. Guise, and J. B. Chaudhuri. "A Comparison of the Denaturants Urea and Guanidine Hydrochloride on Protein Refolding." Food and Bioproducts Processing 75, no. 1 (1997): 50–56. http://dx.doi.org/10.1205/096030897531360.

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3

Milyaeva, Olga Yu, Richard A. Campbell, Shi-Yow Lin, et al. "Synergetic effect of sodium polystyrene sulfonate and guanidine hydrochloride on the surface properties of lysozyme solutions." RSC Advances 5, no. 10 (2015): 7413–22. http://dx.doi.org/10.1039/c4ra14330b.

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A study of the dilational surface viscoelastic properties of mixed solutions of lysozyme and denaturants allows us to characterize the changes of protein tertiary structure in the surface layer upon adsorption at the liquid–gas interface.

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4

Yang, Ya-Wun, and Chi-Cheng Teng. "Stability of polyomavirus major capsid protein VP1 under denaturants guanidine hydrochloride and urea." International Journal of Biological Macromolecules 22, no. 2 (1998): 81–90. http://dx.doi.org/10.1016/s0141-8130(97)00091-3.

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5

Kujo, Chizu, and Toshihisa Ohshima. "Enzymological Characteristics of the Hyperthermostable NAD-Dependent Glutamate Dehydrogenase from the Archaeon Pyrobaculum islandicum and Effects of Denaturants and Organic Solvents." Applied and Environmental Microbiology 64, no. 6 (1998): 2152–57. http://dx.doi.org/10.1128/aem.64.6.2152-2157.1998.

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ABSTRACT NAD-dependent glutamate dehydrogenase (l-glutamate:NAD oxidoreductase, deaminating; EC 1.4.1.2 ) was purified to homogeneity from a crude extract of the continental hyperthermophilic archaeonPyrobaculum islandicum by two successive Red Sepharose CL-4B affinity chromatographies. The enzyme is the most thermostable NAD-dependent dehydrogenase found to date; the activity was not lost after incubation at 100°C for 2 h. The enzyme activity increased linearly with temperature, and the maximum was observed at ca. 90°C. The enzyme has a molecular mass of about 220 kDa and consists of six subu

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6

Gupta, P., A. K. Verma, and P. Chaudhuri (Chattopadhyay). "Investigating the Chaperoning Effect of Nanoparticles in Chemically Denatured zDHFR: An in vitro Study." Asian Journal of Chemistry 33, no. 8 (2021): 1929–34. http://dx.doi.org/10.14233/ajchem.2021.23372.

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Maintenance of native structure and function of the protein is a major concern for industrial production of aggregation prone therapeutically important recombinant proteins. Aggregation may results due to change in the native conformation of proteins under different stress conditions. To overcome the problem of protein aggregation, role of silver and gold nanoparticles have been investigated. The nanoparticles owing to their affirmative interaction with the proteins possess chaperoning activities and protect the native state from denaturation. In the present study, through performing chemical

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7

SINGH, R. Rajesh, and Jui-Yoa CHANG. "Investigating conformational stability of bovine pancreatic phospholipase A2: a novel concept in evaluating the contribution of the native-framework of disulphides to the global conformational stability of proteins." Biochemical Journal 377, no. 3 (2004): 685–92. http://dx.doi.org/10.1042/bj20030968.

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Bovine pancreatic PLA2 (phospholipase A2) is a 14 kDa protein whose structure is highly cross-linked by seven disulphide bonds. We investigated the structural stability of this enzyme by the method of ‘disulphide-scrambling’ with denaturants such as urea, GdmCl (guanidine hydrochloride), GdmSCN (guanidine thiocyanate) and at high temperatures in the presence of 2-mercaptoethanol (0.2 mM) as thiol initiator. Reverse-phase HPLC was used to follow denaturation. To denature 50% of the native protein, 1.25 M GdmSCN, approx. 3 M GdmCl and higher than 8 M urea were required. Only 20% of the protein w

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FAN, Ying-xin, Ming JU, Jun-mei ZHOU, and Chen-lu TSOU. "Activation of chicken liver dihydrofolate reductase by urea and guanidine hydrochloride is accompanied by conformational change at the active site." Biochemical Journal 315, no. 1 (1996): 97–102. http://dx.doi.org/10.1042/bj3150097.

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It has been reported that the activation of dihydrofolate reductase (DHFR) from L1210 mouse leukaemia cells by KCl or thiol modifiers is accompanied by increased digestibility by proteinases [Duffy, Beckman, Peterson, Vitols and Huennekens (1987) J. Biol. Chem. 262, 7028–7033], suggesting a loosening up of the general compact structure of the enzyme. In the present study, the peptide fragments liberated from the chicken liver enzyme by digestion with trypsin in dilute solutions of urea or guanidine hydrochloride (GuHCl) have been separated by FPLC and sequenced. The sequences obtained are uniq

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9

Hovorka,, Štěpán, Vladimír Dohnal,, Ernesto Carrillo-Nava,, and Miguel Costasa. "Infinite dilution activity coefficients for benzene and toluene in water and in aqueous solutions of the protein denaturants urea and guanidine hydrochloride." Journal of Chemical Thermodynamics 32, no. 12 (2000): 1683–705. http://dx.doi.org/10.1006/jcht.2000.0706.

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10

Tang, Hong-Min, Wen-Bin Ou, and Hai-Meng Zhou. "Effects of lactic acid and NaCl on creatine kinase from rabbit muscle." Biochemistry and Cell Biology 81, no. 1 (2003): 1–7. http://dx.doi.org/10.1139/o02-168.

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The lactic acid induced unfolding and the salt-induced folding of creatine kinase (CK) were studied by enzyme activity, fluorescence emission spectra, circular dichroism spectra, and native polyacrylamide gel electrophoresis. The results showed that the kinetics of CK inactivation was a monophase process. Lactic acid caused inactivation and unfolding of CK with no aggregation during CK denaturation. The unfolding of the whole molecule and the inactivation of CK in solutions of different concentration of lactic acid were compared. Much lower lactic acid concentration values were required to bri

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Dissertations / Theses on the topic "Guanidine hydrochloride; Denaturants"

1

Grimshaw, Shaun B. "Novel approaches to characterising native and denatured proteins by NMR." Thesis, University of Oxford, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.301516.

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