• Bulletin of the Korean Chemical Society
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• v.35 no.4
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• pp.1029-1035
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• 2014

The protolytic dissociation process of hydrochloric acid (HCl) and hydrofluoric acid (HF) is studied using the B3LYP and MP2 methods with the 6-311+G(d,p) basis set in the gas phase and in aqueous solution. To study the phenomena in detail, discrete and discrete/continuum models were applied by placing water molecules in various positions around the acid. The dissociation process was studied using the thermodynamic cycle involving the structures optimized both in the gas phase and in aqueous solution and was analyzed with two key energy factors, relaxation free energy (${\Delta}G_{Rex(g)}$) and solvation free energy (${\Delta}G_s$). Based on the results, we could understand the dissociation mechanism and wish to propose the best way to study acid dissociation process using the CPCM methodology in aqueous solution.

• YAKHAK HOEJI
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• v.8 no.3
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• pp.62-68
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• 1964

Author has determined the dissociation velocity constant of carboxyhemoglobin in cattle blood solution by addition of ascorbic acid at $36-38{\deg}.$ It was found that these kinetic data are concordant with Roughton's equation d[COHb]/dt = $m^{'}[CO][O_{2}Hb]/[O_{2}$ - m[COHb] and that the dissociation velocity constant of carboxyhemoglobin was accelerated by the presence of ascorbic acid from 0.119 to 0.135.

• Journal of the Korean Chemical Society
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• v.33 no.4
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• pp.343-349
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• 1989

The dissociation constants of ${\beta}$-alanine and ${\gamma}$-aminobutyric acid were measured in the temperature range from 20 to $40^{\circ}C$ and pressure up to 2,500 bar by conductometric method. The both dissociation constants of respective amino acid increase with temperature increase but pressure effect is not same as the temperature. The $K_1$ increases as pressure increases but $K_2$ decreases. The properties of these amino acids were discussed in terms of the thermodynamic properties of the dissociation reaction. A relationship between the dissociation constants and the distance between substituted groups of amino acid was discussed. The substituted effects of the reaction were deduced from Hammett reaction and substituted constants which were calculated from the measured dissociation constants.

• BMB Reports
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• v.38 no.5
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• pp.533-538
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• 2005

The kinetics of thermal dissociation of superoxide dismutase (SOD) was studied in 0.05 M Tris-HCl buffer at pH 7.4 containing $10^{-4}\;M$ EDTA. The number of conformational locks and contact areas and amino acid residues of dimers of SOD were obtained by kinetic analysis and biochemical calculation. The cleavage bonds between dimers of SOD during thermal dissociation and type of interactions between specific amino acid residues were also simulated. Two identical contact areas between two subunits were identified. Cleavage of these contact areas resulted in dissociation of the subunits, with destruction of the active centers, and thus, lost of activity. It is suggested that the contact areas interact with active centers by conformational changes involving secondary structural elements.

• Mass Spectrometry Letters
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• v.10 no.4
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• pp.117-122
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• 2019

This study demonstrated the sensitivity of electron capture dissociation mass spectrometry (ECD-MS) to probe subtle conformational changes in gaseous melittin ions induced by the substitution of an amino acid. ECD-MS was performed for triply and quadruply-protonated melittin and its variants obtained by a single amino acid substitution, namely, D-Pro14, Pro14Ala, and Leu13Ala. Although native triply-protonted melittin showed only a few peptide backbone cleavage products, the D-Pro14 and Pro14Ala variants exhibited extensive backbone fragments, suggesting the occurrence of a significant structural or conformational change induced by a single amino acid substitution at Pro14. On the contrary, the substitution at Leu13, namely Leu13Ala (+3), did not cause significant changes in the ECD backbone fragmentation pattern. Thus, the sensitivity of ECD-MS is demonstrated to be good enough to probe the aforementioned conformational change in melittin.

• Bulletin of the Korean Chemical Society
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• v.19 no.6
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• pp.671-676
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• 1998

The formation and dissociation rates of $Ce^{3+}$ Complexes of the 1,4,7,10-tetraaza-13,16-dioxacyclooctadecane-NN', N",N"'-tetraacetic acid (1), 1,4,7,10-tetraaza-13,16-dioxacyclooctadecane-N,N',N",N"'-tetramethylacetic acid (2), and 1,4,7,10-tetraaza-13,16-dioxacyclooctadecane-N,N',N",N"'-tetrapropionic acid (3) have been measured by the use of stopped-flow spectrophotometry. Observations were made at 25.0±0.1 ℃ and at an ionic strength of 0.10 M $NaClO_4$. The complexation of $Ce^{3+}$ ion with 1 and 2 proceeds through the formation of an intermediate complex $(CeH_3L^{2+})^*$ in which the $Ce^{3+}$ ion is incompletely coordinated. This may then lead to be a final product in the rate-determining step. Between pH 4.76 and 5.76, the diprotonated $(H_2L^{2-})$ from is revealed to be a kinetically active species despite of its low concentration. The stability constants $(logK(CeH_3L^{2+}))$ and specific water-assisted rate constants $(k_{OH})$ of intermediate complexes have been determined from the kinetic data. The dissociation reactions of $Ce^{3+}$ complexes of 1, 2, and 3 were investigated with $Cu^{2+}$, ions as a scavenger in acetate buffer. All complexes exhibit acid-independent and acid-catalyzed contributions. The effect of buffer and $Cu^{2+}$ concentration on the dissociation rate has also been investigated. The ligand effect on the dissociation rate of $Ce^{3+}$ complexes is discussed in terms of the side-pendant arms and the chelate ring sizes of the ligands.

• Archives of Pharmacal Research
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• v.16 no.3
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• pp.180-185
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• 1993

The acid dissociation constants of certain Schiff bases derived from isatin with p-substituted benzoyl hydrazines and somee amino acids of glycine, $\beta$-and $\alpha$-alanine, valine, $\beta$-phenyl-$\alpha$-alanine and anthranilic acid have been detemined potentiometrically at different temperatures in different aquo-organic solvent mixtures (ethnol, dioxane, dimethyl formamide, methanol, acetone and tetrahydrofurance). The pKa values were demonstrated on the light of the different electornic and steric effects of the substituents and the sovlent characteristics. In all the mixed media used, ionization of the compounds decreased by increasing the mole fraction of the organic cosolvent. Theemodynamic parameters $(\Delta{H}^\circ,\;\Delta{G}^\circ,\;\Delta{S}^\circ)$ were evaluated. The structural effects of the investigated compounds on these parameters were reported and discussed.

• Mass Spectrometry Letters
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• v.1 no.1
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• pp.5-8
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• 2010

In the present study, collisionally-activated dissociation (CAD) experiments were performed under low energy collision conditions in six peptides containing a disulfide bond. Fragments produced as a result of the cleavage of a disulfide bond were obtained after CAD in four peptides (bactenecin, TGF-$\alpha$, cortistantin, and linearly linked peptide, Scheme 1) with basic amino acid residues. In contrast, the CAD analysis of two peptides with no basic residue (oxytocin and tocinoic acid) rarely produced fragments indicative of cleavage of a disulfide bond. These results are consistent with the mobile proton model suggested by the McLuckey and O'air groups (ref. 22 and 23); nonmobile protons sequestered at basic amino acid residues appear to promote the cleavage of disulfide bonds.

• YAKHAK HOEJI
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• v.9 no.1_2
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• pp.4-7
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• 1965

Acid dissociation constants of sulfamethoxypyridazine, sulfadimethoxine, sulfamerazine, sulfathiazole and sulfadiazine, and stability constants for formation of copper chelate were calculated from their titration curves in 80% dimethylformamide with ionic strength 0.1 at $25{\deg}$ It was found that the acid dissociation constants (pKa) of sulfa-drugs were in the range of 9.33 - 10.05, and the stability constants (log $k_{1}$, $k_{2})$ of their copper chelates were in the range of 9.33-9.71.

• Bulletin of the Korean Chemical Society
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• v.33 no.12
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• pp.4255-4257
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• 2012