PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2110472-5 1990 This suggests that the unfolded conformations of RNase A become more accessible to urea as the net charge on the molecule increases. Urea 83-87 ribonuclease A family member 1, pancreatic Homo sapiens 49-56 8465956-0 1993 C-terminal labeling of ribonuclease A with an extrinsic fluorescent probe by carboxypeptidase Y-catalyzed transpeptidation in the presence of urea. Urea 142-146 ribonuclease A family member 1, pancreatic Homo sapiens 23-37 3622771-2 1987 Proton chemical shift variations with temperature, addition of stabilizing (TFE) or denaturing agents (urea) provide a strong experimental basis for concluding that in aqueous solution this RNase fragment forms an alpha-helix structure similar to that in the intact RNase A crystal. Urea 103-107 ribonuclease A family member 1, pancreatic Homo sapiens 266-273 4052411-2 1985 First, by use of a double-jump technique, it is demonstrated that a similar nativelike intermediate exists on the major slow-folding pathway of both urea- and Gdn.HCl-denatured RNase A. Urea 149-153 ribonuclease A family member 1, pancreatic Homo sapiens 177-184 29272129-10 2018 However, urea subverts the Glu-induced intermediate formed by alpha-LA, whereas it only slightly destabilizes in the case of RNase A which has a positive surface charge and could possess charge-charge interactions with Glu. Urea 9-13 ribonuclease A family member 1, pancreatic Homo sapiens 125-132 30451257-1 2018 DSC measurements on RNase A at neutral pH show that five stabilizing agents, namely trimethylamine N-oxide, glucose, sucrose, betaine and sodium sulfate, can counteract the destabilizing action of urea, sodium perchlorate, guanidinium chloride and guanidinium thiocyanate. Urea 197-201 ribonuclease A family member 1, pancreatic Homo sapiens 20-27 27320838-0 2016 Alanine Counteracts the Destabilizing Effect that Urea has on RNase-A. Urea 50-54 ribonuclease A family member 1, pancreatic Homo sapiens 62-69 27320838-4 2016 OBJECTIVE: We investigated the behavior of a non-methylamine osmolyte, alanine for its counteracting effect against urea denaturation of a model protein, ribonuclease A (RNase-A). Urea 116-120 ribonuclease A family member 1, pancreatic Homo sapiens 170-177 27320838-5 2016 METHODS: We have measured structure and thermodynamic parameters (Tm, DeltaHm, and DeltaGD ) of RNase-A in the presence of alanine, urea and their combination. Urea 132-136 ribonuclease A family member 1, pancreatic Homo sapiens 96-103 27320838-7 2016 RESULTS: We observed that alanine but not glycine counteracts urea"s harmful effect on RNase-A stability. Urea 62-66 ribonuclease A family member 1, pancreatic Homo sapiens 87-94 20085318-4 2010 Using UV difference, near UV circular dichroism, folding kinetics, and multidimensional heteronuclear NMR spectroscopy, the conformation of RNase A in 40% acetic acid and in 8 M urea has been characterized. Urea 178-182 ribonuclease A family member 1, pancreatic Homo sapiens 140-147 21261048-3 2010 The results indicated that the reduced/ denatured RNase A can be refolded completely under the optimized conditions of pH 8.0, 2.0 mol/L urea and the concentration ratio of GSH/GSSG of 8: 1 in mobile phase. Urea 137-141 ribonuclease A family member 1, pancreatic Homo sapiens 50-57 21261048-4 2010 When the denatured protein was at the concentration of 5.0 mg/mL, the bioactivity efficiency and mass recoveries were 98.0% and 61.9% for 8.0 mol/L urea-denatured RNase A, respectively; and 100.1% and 66.8% for 7.0 mol/L guanidine hydrochloride (GuaHCl)-denatured RNase A, respectively. Urea 148-152 ribonuclease A family member 1, pancreatic Homo sapiens 163-170 21261048-4 2010 When the denatured protein was at the concentration of 5.0 mg/mL, the bioactivity efficiency and mass recoveries were 98.0% and 61.9% for 8.0 mol/L urea-denatured RNase A, respectively; and 100.1% and 66.8% for 7.0 mol/L guanidine hydrochloride (GuaHCl)-denatured RNase A, respectively. Urea 148-152 ribonuclease A family member 1, pancreatic Homo sapiens 264-271 23381689-2 2013 Based in enzyme kinetics experiments and (1)H NMR spectroscopic analysis we proposed that urea, at low concentrations, directly interacts with the protonated histidines of the active center of RNase A, following a simple model of competitive inhibition. Urea 90-94 ribonuclease A family member 1, pancreatic Homo sapiens 193-200 23381689-5 2013 Also, our results would explain the observed disruption of the (1)H NMR signals corresponding to H12 and H119 (involved in catalysis) of the RNase A studied in the presence of urea. Urea 176-180 ribonuclease A family member 1, pancreatic Homo sapiens 141-148 20085318-7 2010 I(N) is known to be populated during RNase A refolding following denaturation in concentrated solutions of urea or guanidinium chloride, and we find that urea- or GdmCl-denatured RNase A can oligomerize during refolding. Urea 107-111 ribonuclease A family member 1, pancreatic Homo sapiens 179-186 20085318-7 2010 I(N) is known to be populated during RNase A refolding following denaturation in concentrated solutions of urea or guanidinium chloride, and we find that urea- or GdmCl-denatured RNase A can oligomerize during refolding. Urea 154-158 ribonuclease A family member 1, pancreatic Homo sapiens 179-186 17559285-2 2007 Urea denaturation analyses showed that the thermodynamic stability of RNase A decreased upon adsorption onto the nanoparticles, with greater decrease on larger nanoparticles. Urea 0-4 ribonuclease A family member 1, pancreatic Homo sapiens 70-77 19580327-2 2009 On the basis of kinetic evidence at low urea concentrations, (1)H NMR spectroscopic analysis, and molecular orbital calculations, we propose a mechanistic model for the denaturation of RNase A in urea. Urea 40-44 ribonuclease A family member 1, pancreatic Homo sapiens 185-192 19580327-2 2009 On the basis of kinetic evidence at low urea concentrations, (1)H NMR spectroscopic analysis, and molecular orbital calculations, we propose a mechanistic model for the denaturation of RNase A in urea. Urea 196-200 ribonuclease A family member 1, pancreatic Homo sapiens 185-192 15886035-0 2005 A comparison of the counteracting effects of glycine betaine and TMAO on the activity of RNase A in aqueous urea solution. Urea 108-112 ribonuclease A family member 1, pancreatic Homo sapiens 89-96 17633529-5 2007 The biphasic dependence of the rate of H-D exchange and proteolytic degradation of RNase A on urea concentration is also explained by the combination of local and global fluctuations. Urea 94-98 ribonuclease A family member 1, pancreatic Homo sapiens 83-90 16884715-2 2006 Copper complexes of (-)-epicatechin gallate and (-)-epigallocatechin gallate were found to inhibit the enzymatic activity of Ribonuclease A (RNase A) as revealed by an agarose gel based assay and urea denatured gel electrophoresis. Urea 196-200 ribonuclease A family member 1, pancreatic Homo sapiens 125-139 16884715-2 2006 Copper complexes of (-)-epicatechin gallate and (-)-epigallocatechin gallate were found to inhibit the enzymatic activity of Ribonuclease A (RNase A) as revealed by an agarose gel based assay and urea denatured gel electrophoresis. Urea 196-200 ribonuclease A family member 1, pancreatic Homo sapiens 141-148 15886035-3 2005 As part of a project to explain and understand the action of these methylamines, the RNase A-catalysed degradation of polyuridylic acid in the presence of urea and various osmolytes (0-1.0 M) was studied using (31)P Nuclear Magnetic Resonance spectroscopy. Urea 155-159 ribonuclease A family member 1, pancreatic Homo sapiens 85-92 15886035-5 2005 These results indicate that the modification of RNase A activity induced by urea is not associated with gross irreversible structural changes and that both glycine betaine and trimethylamine-N-oxide have kinetically detectable counteracting effects. Urea 76-80 ribonuclease A family member 1, pancreatic Homo sapiens 48-55 14691228-3 2004 The unfolded state of RNase A in a 2.4 M urea solution at pH 3.0 became native in conformation and compactness by the addition of 35% PEG 20000 or Ficoll 70. Urea 41-45 ribonuclease A family member 1, pancreatic Homo sapiens 22-29 9575901-6 1998 To test another macromolecule, we now compare GPC and betaine in counteracting reduction of the thermal stability of Rnase A by urea. Urea 128-132 ribonuclease A family member 1, pancreatic Homo sapiens 117-124 10862769-1 2000 31P NMR spectroscopy has been used to show that the activity of RNase A, which is lowered in the presence of urea, can be recovered with trimethylamine-N-oxide (TMAO). Urea 109-113 ribonuclease A family member 1, pancreatic Homo sapiens 64-71 10211829-2 1999 The results show that the thermal stability of RNase A decreases with increasing concentration of denaturants and the size of the hydrophobic group substituted on the urea molecule. Urea 167-171 ribonuclease A family member 1, pancreatic Homo sapiens 47-54 10036174-8 1999 These methods allow analysis and construction of the denaturation curves of RNase A in the presence of urea, GdmCl and GdmSCN. Urea 103-107 ribonuclease A family member 1, pancreatic Homo sapiens 76-83 12741842-4 2003 Addition of TMAO to urea solutions containing RNase A also suppresses HX rate constants. Urea 20-24 ribonuclease A family member 1, pancreatic Homo sapiens 46-53 12741842-7 2003 RNase A is so resistant to urea denaturation at pH* 6.35 that even in the presence of 4.8 M urea, the native ensemble accounts for >99.5% of the protein. Urea 27-31 ribonuclease A family member 1, pancreatic Homo sapiens 0-7 12741842-7 2003 RNase A is so resistant to urea denaturation at pH* 6.35 that even in the presence of 4.8 M urea, the native ensemble accounts for >99.5% of the protein. Urea 92-96 ribonuclease A family member 1, pancreatic Homo sapiens 0-7 12741842-10 2003 Under these experimental conditions, the use of DeltaG(HX) as a basis for HX analysis of RNase A urea denaturation is invalid. Urea 97-101 ribonuclease A family member 1, pancreatic Homo sapiens 89-96 8961946-0 1996 Refolding of thermally and urea-denatured ribonuclease A monitored by time-resolved FTIR spectroscopy. Urea 27-31 ribonuclease A family member 1, pancreatic Homo sapiens 42-56 8961946-7 1996 Therefore, our kinetic infrared studies provide evidence for a high structural similarity of urea-denatured and heat-denatured RNase A, corroborating the conclusions derived from the direct comparison of the infrared spectra of thermally and chemically denatured RNase A under equilibrium conditions [Fabian, H., & Mantsch, H.H. Urea 93-97 ribonuclease A family member 1, pancreatic Homo sapiens 263-270 8961946-9 1996 In detail, the kinetic infrared data demonstrate that in the time window of 0.1-30 s approximately 40% of the native beta-sheet structure in RNase A is formed in the presence of 0.6 M urea at pH* 3.6, indicating that up to 60% of the beta-structure is formed out of the time window used in this study. Urea 184-188 ribonuclease A family member 1, pancreatic Homo sapiens 141-148