Effect of temperature on the stability constants of chloro complexes of actinyl ions

1983 ◽  
Vol 78 (2) ◽  
pp. 319-325 ◽  
Author(s):  
L. Bednarczyk ◽  
I. Fidelis
Keyword(s):  
Stability Constants ◽  
Effect Of Temperature ◽  
Chloro Complexes ◽  
The Stability

Effect of temperature on the stability constants of zinc- nitrilotriacetic acid- ammonia system

2018 ◽  
Vol 181 ◽  
pp. 97-102 ◽  
Author(s):  
Tianzu Yang ◽  
Boyi Xie ◽  
Lin Chen ◽  
Zhandong Hao ◽  
Duchao Zhang ◽  
...  
Keyword(s):  
Stability Constants ◽  
Nitrilotriacetic Acid ◽  
Effect Of Temperature ◽  
The Stability

Potentiometric and thermodynamic studies of 3-methyl-1-phenyl-{p-[N-(pyrimidin-2-yl)-sulfamoyl]phenylazo}-2-pyrazolin-5-one and its metal complexes

2006 ◽  
Vol 60 (1) ◽  
Author(s):  
A. Fouda ◽  
A. Al-Sarawy ◽  
E. El-Katori
Keyword(s):  
Transition Metal ◽  
Metal Complexes ◽  
Stability Constants ◽  
Dissociation Constants ◽  
Transition Metal Ions ◽  
Effect Of Temperature ◽  
Water Mixture ◽  
Dissociation Process ◽  
The Stability ◽  
Metal Ligand

AbstractThe dissociation constants of 3-methyl-1-phenyl-{p-[N-(pyrimidin-2-yl)sulfamoyl]phenylazo}-2-pyrazolin-5-one and metal-ligand stability constants of its complexes with some transition metal ions have been determined potentiometrically in 0.1 M-KCl and ethanol—water mixture (30 vol. %). The order of the stability constants of the formed complexes increases in the sequence Mn2+, Co2+, Ni2+, Cu2+, La3+, Hf3+, UO22+, Zr4+. The effect of temperature was studied and the corresponding thermodynamic parameters (ΔG, ΔH, and ΔS) were derived and discussed. The dissociation process is nonspontaneous, endothermic, and entropically unfavourable. The formation of the metal complexes was found to be spontaneous, exothermic, and entropically favourable.

Complex Formation in Molten Salts Studied by Distribution Methods

1963 ◽  
Vol 18 (7) ◽  
pp. 840-842 ◽  
Author(s):  
J. O. Liljenzin ◽  
H. Reinhardt ◽  
H. Wirries ◽  
R. Lindner
Keyword(s):  
Complex Formation ◽  
Stability Constants ◽  
Molten Salts ◽  
Chloro Complexes ◽  
Complex Constant ◽  
The Stability

With a distribution technique described earlier the stability constants of cadmium-chloro complexes were evaluated. The values obtained are practically identical with those obtained by other authors with polarographic methods with the exception of the first complex constant which was found to be considerably higher (832) than that described in the literature (200).

Modelling the Effect of Temperature on the Stability of Bromide and Carbonate Complexes of Europium, Gadolinium, Terbium and Determination of their Thermodynamic Functions

2021 ◽  
Vol 1031 ◽  
pp. 103-108
Author(s):  
Igor Fialkovsky ◽  
Denis Lutskiy ◽  
Andrey Alekseev ◽  
Alexey Blinov
Keyword(s):  
Linear Regression ◽  
Stability Constants ◽  
Thermodynamic Functions ◽  
Outer Sphere ◽  
Regression Equation ◽  
Effect Of Temperature ◽  
Enthalpies Of Formation ◽  
Linear Regression Equation ◽  
The Stability ◽  
Carbonate Complexes

A method has been developed for calculating the stability constants of inorganic complexes of rare-earth metals at various temperatures, based on analysis of the literature data by obtaining a linear regression equation on the form: . Using this method, the stability constants of bromide LnBr2+ and carbonate LnCO3+ complexes of europium, terbium, and gadolinium in aqueous solutions at temperatures of 50, 75, and 100 ° C were obtained. The obtained values of the coefficients А(T1) and В(T1) of the linear regression equation can be used to calculate the stability constants of complexes of europium, terbium, and gadolinium with other inorganic ligands at given temperatures. Based on the temperature dependence of the stability constants of bromide and carbonate complexes, their standard entropies and enthalpies of formation were calculated. Based on the obtained values of the thermodynamic functions, an assumption was made about the outer-sphere or inner-sphere nature of the complex.

Applicability of Instability Index for In vitro Protein Stability Prediction

2019 ◽  
Vol 26 (5) ◽  
pp. 339-347 ◽  
Author(s):  
Dilani G. Gamage ◽  
Ajith Gunaratne ◽  
Gopal R. Periyannan ◽  
Timothy G. Russell
Keyword(s):  
Protein Stability ◽  
Caulobacter Crescentus ◽  
Effect Of Temperature ◽  
Instability Index ◽  
Dipeptide Composition ◽  
Experimental Conditions ◽  
The Stability ◽  
Vitro Protein

Background: The dipeptide composition-based Instability Index (II) is one of the protein primary structure-dependent methods available for in vivo protein stability predictions. As per this method, proteins with II value below 40 are stable proteins. Intracellular protein stability principles guided the original development of the II method. However, the use of the II method for in vitro protein stability predictions raises questions about the validity of applying the II method under experimental conditions that are different from the in vivo setting. Objective: The aim of this study is to experimentally test the validity of the use of II as an in vitro protein stability predictor. Methods: A representative protein CCM (CCM - Caulobacter crescentus metalloprotein) that rapidly degrades under in vitro conditions was used to probe the dipeptide sequence-dependent degradation properties of CCM by generating CCM mutants to represent stable and unstable II values. A comparative degradation analysis was carried out under in vitro conditions using wildtype CCM, CCM mutants and two other candidate proteins: metallo-β-lactamase L1 and α -S1- casein representing stable, borderline stable/unstable, and unstable proteins as per the II predictions. The effect of temperature and a protein stabilizing agent on CCM degradation was also tested. Results: Data support the dipeptide composition-dependent protein stability/instability in wt-CCM and mutants as predicted by the II method under in vitro conditions. However, the II failed to accurately represent the stability of other tested proteins. Data indicate the influence of protein environmental factors on the autoproteolysis of proteins. Conclusion: Broader application of the II method for the prediction of protein stability under in vitro conditions is questionable as the stability of the protein may be dependent not only on the intrinsic nature of the protein but also on the conditions of the protein milieu.

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