Thermochemical Properties of Some Carboxylic Acids, Amines, and N-Substituted Amides in Aqueous Solution.

Konicek, Jiri; Wadsö, Ingemar; Jamison, Warren E.; Andresen, Arne F.; Engebretsen, Jan E.; Ehrenberg, L.

doi:10.3891/acta.chem.scand.25-1541

Cited by 148 publications

(50 citation statements)

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“…The average value D solv H 1 m ½CONH ¼ ðÀ61:7 AE 2:8Þ kJ Á mol À1 obtained was almost identical to that given by summation of the molar solvation enthalpies of CO and NH functional groups from our earlier solvation data for alkylketones [14] and from the literature data for alkylamines [29,30], namely (À61.2 ± 1.5) kJ AE mol À1 (table 8). Moreover, these data are in good agreement with those calculated by subtracting from the molar enthalpies of solvation of linear small peptides the enthalpies of solvation of the alkanes with the same number of C atoms as in the amino acid side chains [23,27,28,30] (3): the literature data were also used by Lilley who obtained D solv H 1 m ½CONH ¼ ðÀ52:3 AE 2:5Þ kJ Á mol À1 [31].…”

Section: Enthalpy Of Solvation Of the Conhá á áConh Functional Groupsupporting

confidence: 66%

Thermodynamics of solvation of some small peptides in water at T=298.15K

Gatta

Усачева

Badea

et al. 2006

The Journal of Chemical Thermodynamics

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Section: Enthalpy Of Solvation Of the Conhá á áConh Functional Groupsupporting

confidence: 66%

Thermodynamics of solvation of some small peptides in water at T=298.15K

Gatta

Усачева

Badea

et al. 2006

The Journal of Chemical Thermodynamics

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“…The heat capacity of the crystalline phase was also measured at T = 298.15 K using a non-commercial high-precision drop calorimeter (University of Porto) and the drop method, which is described in detail in [25][26][27]. The apparatus comprises two main parts: a furnace for temperature equilibration of the sample ampoule and a calorimetric receiving block based on a twin heat conduction type.…”

Section: University Of Portomentioning

confidence: 99%

Recommended vapor pressure and thermophysical data for ferrocene

Fulem

Růžička

Červinka

et al. 2013

The Journal of Chemical Thermodynamics

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“…It was not possible to determine calorimetrically a reliable experimental A C , value for the transfer of biotin between water and a nonaqueous environment like ethanol but results from model studies may be used to construct a reasonable A C , value for such a process. From recent calorimetric studies [7] involving RCOOH, RNH,, ROH, RCONHR' it was found that dC, for the transfer of a CH, group (n = 0, 1, 2, 3) from aqueous solution to the medium of the pure compound in its liquid aggregation state was about -15 cal x mol CH,-l x K-l. The value was not significantly affected by the presence of the functional groups.…”

Section: Discussionmentioning

confidence: 99%

Thermochemistry of the Avidin‐Biotin Reaction

Suurkuusk¹,

Wadsö²

1972

European Journal of Biochemistry

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The enthalpy for the binding of biotin to avidin has been determined a t 25, 34 and 43 "C (pH 9, ammonium acetate buffer): AH (25 "C) = -22.5 f 0.1 kcal/mol biotin; AC,, = -237 &-12 cal x mol biotin-l x K-l.Solubilities and enthalpies of solution of biotin in water and in ethanol were determined at 25 "C. The transfer process for biotin between water and ethanol was considered as a simple model for the protein binding process.The properties of avidin and the nature of the avidin-biotin binding reaction have been studied extensively, in particular by Green and coworkers [l-51. It was shown that avidin has four identical and independent binding sites for biotin. The standard free energy of binding, AGO, was determined to be -20.5 kcal/mole biotin and from calorimetric measurements around 25 "C, the corresponding enthalpy change was found to be within uncertainty limits the same. AH was shown to be independent of pH (between 5 and 9) and independent of the buffer used [3].I n the present work, some of Green's calorimetric measurements have been repeated. Measurements were further extended to three well-defined temperatures in order to arrive a t a A C,, value for the process.Solubilities and calorimetric enthalpies of solution of biotin in water and in ethanol were determined. From the results of these measurements, AH and AS for the transfer of biotin between water and ethanol were calculated. This transfer process may be looked upon as a simple model for the studied biotin-avidin binding reaction. EXPERIMENTAL PROCEDURE MaterialsAvidin was purchased from Worthington (Freehold, NewJersey, U.S.A.) and was used without further purification (lot No. Av IAA; 11.6 unitslg). Avidin solutions were freshly prepared for each experiment.Biotin (puriss grade, BDH) was further purified by recrystallization from water. The crystals were Presented in part at First European Biophysics Congress, Baden (Wien) 1971. dried in air a t I10 "C for 12 h after which they were vacuum treated for 24 h a t room temperature. Alkaline titration gave an equivalent weight of 244.8 6 0.2 (99.5°/0).Glass-distilled water was used in the preparation of the calorimetric solutions. Ammonium acetate, used as buffer substance in the calorimetric experiments, was of analytical grade (BDH). I n the solution experiments, 99.5O/, ethanol was used. No impurities could be detected by gas chromatography. Calorimetric Equipment and ProcedureFor the protein-binding experiments an LKB 10700-2 batch microcalorimeter was used. The instrument was fitted with reaction cells of 18-carat gold. The compartments in one of the cells were charged with 2 and 4 ml of avidin and biotin solution, respectively. The reference cell was charged with the same quantities of buffer solution. For each calorimetric run, both cells were treated in the same manner with respect to rinsing and charging procedures.Measurements were made at three temperatures, 25, 34 and 43 "C, respectively. The exact reaction temperatures were determined by means of a Calibrated thermistor placed inside t...

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Thermochemical Properties of Some Carboxylic Acids, Amines, and N-Substituted Amides in Aqueous Solution.

Cited by 148 publications

References 0 publications

Thermodynamics of solvation of some small peptides in water at T=298.15K

Thermodynamics of solvation of some small peptides in water at T=298.15K

Recommended vapor pressure and thermophysical data for ferrocene

Thermochemistry of the Avidin‐Biotin Reaction

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