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 (September 15, 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 substantially. A study of the unfolding of three single-tryptophan mutant forms of iRFP713 expectedly revealed that protein unfolding begins with the dissociation of the native dimer, while the monomers remain compact. A further increase in the denaturant concentration leads to the formation of an intermediate state of iRFP713 having hydrophobic areas exposed on the protein surface (I). The total surface charge of iRFP713 (pI 5.86) changes from negative to positive with an increase in the concentration of GdnHCl and GTC because the negative charge of glutamic and aspartic acids is neutralized by forming salt bridges between the carboxyl groups and GdnH+ ions and because the guanidinium cations bind to amide groups of glutamines and asparagines. The coincidence of both the concentration of the denaturants at which the intermediate state of iRFP713 accumulates and the concentration of GdnH+ ions at which the neutralization of the surface charge of the protein in this state is ensured results in strong protein aggregation. This is evidently realized by iRFP713 unfolding by GTC. At the unfolding of the protein by GdnHCl, an intermediate state is populated at higher denaturant concentrations and a strong aggregation is not observed. As expected, protein aggregates are not formed in the presence of the urea. The aggregation of the protein upon neutralization of the charge on the macromolecule surface is the main indicator of the intermediate state of protein. The unfolded state of iRFP713, whose formation is accompanied by a significant decrease in the parameter A, was found to have a different residual structure in the denaturants used.
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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 (March 1997): 50–56. http://dx.doi.org/10.1205/096030897531360.

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3

Milyaeva, Olga Yu, Richard A. Campbell, Shi-Yow Lin, Giuseppe Loglio, Reinhard Miller, Michail M. Tihonov, Imre Varga, Anna V. Volkova, and Boris A. Noskov. "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 (April 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 (June 1, 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 subunits with identical molecular masses of 36 kDa. The enzyme required NAD as a coenzyme for l-glutamate deamination and was different from the NADP-dependent glutamate dehydrogenase from other hyperthermophiles. The Km values for NAD,l-glutamate, NADH, 2-oxoglutarate, and ammonia were 0.025, 0.17, 0.0050, 0.066, and 9.7 mM, respectively. The enzyme activity was significantly increased by the addition of denaturants such as guanidine hydrochloride and some water-miscible organic solvents such as acetonitrile and tetrahydrofuran. When fluorescence of the enzyme was measured in the presence of guanidine hydrochloride, a significant emission spectrum change and a shift in the maximum were observed but not in the presence of urea. These results indicate that this hyperthermophilic enzyme may have great potential in applications to biosensor and bioreactor processes.
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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 denaturation of zebrafish dihydrofolate reductase using denaturants like guanidine hydrochloride and urea in the presence and absence of gold and silver nanoparticles and monitoring the process through enzyme activity assay and intrinsic tryptophan fluorescence, we have demonstrated the impact of nanoparticles in maintaining native conformation of proteins. Further, the outcome of refolding studies of DHFR protein with nanoparticles monitored by UV-visible spectroscopy was also reported.
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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 (February 1, 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 was denatured after 2 h at 60 °C, whereas complete denaturation was seen after 2 h at 70 °C and within 30 min at 80 °C. A distinct enhancement of stability was observed when denaturation was conducted in the presence of 10 mM calcium chloride, which has not been reported previously. CD studies of GdmCl denaturation of bovine PLA2 showed that 2.5 M GdmCl was required to denature 50% of the protein in the presence of 0.2 mM 2-mercaptoethanol (in agreement with the HPLC analysis), whereas 6.4 M GdmCl was necessary to denature 50% of the protein in the absence of a thiol initiator. Conformational stability (ΔGwater) was estimated to be 8.7 kcal/mol (1 cal=4.184 J) by ‘disulphide-intact’ denaturation (where ‘native’ disulphide framework was unaffected) and 2.5 kcal/mol by ‘disulphide-scrambling’ denaturation (involved breaking of native disulphides and formation of ‘non-native’ ones). The difference, Δ(ΔGwater), of 6.2 kcal/mol was the conformational stability contributed by the ‘native-framework’ of seven disulphides. Using bovine PLA2 as an example, we have demonstrated a novel comparative technique, where the conformational stability study of a disulphide-containing protein, with a common denaturant, in both the presence and absence of catalytic amounts of a thiol initiator can be used as a convenient method to estimate selectively and quantitatively the actual contribution of the ‘native disulphide bond network’ towards the global conformational stability of the protein.
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8

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 (April 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 unique when compared with the known sequence of DHFR and thus allow the points of proteolytic cleavage identified for the urea- and GuHCl-activated enzyme to be at or near the active site. It was also indicated by the enhanced fluorescence of 2-p-toluidinylnaphthalene 6-sulphonate that conformational changes at the active site in dilute GuHCl parallel GuHCl activation. The above results indicate that the activation of DHFR in dilute denaturants is accompanied by a loosening up of its compact structure especially at or near the active site, suggesting that the flexibility at its active site is essential for the full expression of its catalytic activity.
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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 (December 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 (January 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 bring about inactivation than were required to produce significant conformational changes of the enzyme molecule. At higher concentrations of lactic acid (more than 0.2 mM) the CK dimers were partially dissociated, as proved by native polyacrylamide gel electrophoresis. NaCl induced the molten globule state with a compact structure after CK was denatured with 0.8 mM lactic acid, and the increasing of anions led to a tight side-chain. The above results suggest that the effect of lactic acid differed from that of other denaturants such as guanidine hydrochloride, HCl, or urea during CK folding, and the molten globule state indicates that intermediates exist during CK folding.Key words: lactic acid, creatine kinase, salt-induced, unfolding, molten globule state.
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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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