Apparent molal heat capacities and volumes of amino acids in aqueous polyol solutions

1978 ◽  
Vol 56 (13) ◽  
pp. 1827-1831 ◽  
Author(s):  
Giuseppa DiPaola ◽  
Bernard Belleau
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Aqueous Solutions ◽  
Transfer Functions ◽  
Heat Capacities ◽  
Side Chains ◽  
Dilute Solutions ◽  
Flow Microcalorimeter ◽  
Regular Increase ◽  
Apparent Molal Heat Capacities

Densities (24 °C) and volumetric specific beats (25 °C) were measured for amino acids (0.05–0.5 m) containing apolar side chains in water, and in aqueous solutions of glycerol, mannitol, sorbitol, NaCl, urea, and Gu•HCl, with a flow densimeter and flow microcalorimeter respectively.The derived apparent molal quantifies and transfer functions of the amino acids in aqueous polyol solutions reveal no specificities which might explain the origin of the unique behavior of polyols in protein systems. However, the study did reveal a regular increase in the structure-making ability of the amino acid as the hydrophobicity of the side chains increased. This structure-making tendency was reduced significantly in dilute solutions of the higher polyols.

Apparent molar heat capacities and volumes of some aqueous solutions of aliphatic amino acids at 288.15, 298.15, 313.15, and 328.15 K

1994 ◽  
Vol 72 (2) ◽  
pp. 362-368 ◽  
Author(s):  
Andrew W. Hakin ◽  
Michelle M. Duke ◽  
Sheri A. Klassen ◽  
Robert M. McKay ◽  
Kathryn E. Preuss
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Aqueous Solutions ◽  
Equilibrium Constants ◽  
Heat Capacities ◽  
Apparent Molar Volumes ◽  
Protein Chemistry ◽  
Standard State ◽  
Apparent Molar Heat Capacities ◽  
Molar Volumes

The thermodynamics of amino acid systems are key to the understanding of protein chemistry. We have found that many previous studies of the apparent molar volumes and heat capacities of aqueous solutions of amino acids were conducted at the standard temperature of 298.15 K. This does not allow for the fact that most biological processes occur at temperatures removed from this standard condition.In an attempt to address this imbalance we have measured densities and heat capacities for aqueous solutions of glycine, L-alanine, L-serine, and L-threonine at 288.15, 298.15, 313.15, and 328.15 K using a Picker flow microcalorimeter. Apparent molar volumes and heat capacities, and the associated standard state partial molar properties have been calculated. Constant pressure variations of revised Helgeson, Kirkham, and Flowers equations have been fitted to calculated standard state volumes and heat capacities over the temperature range 288.15 to 328.15 K. These equations may be used to estimate standard state volumes and heat capacities, and hence equilibrium constants, for aqueous amino acid systems at higher temperatures.

The volumetric and thermochemical properties of aqueous solutions of L-valine, L-leucine, and L-isoleucine at 288.15, 298.15, 313.15, and 328.15 K

1994 ◽  
Vol 72 (6) ◽  
pp. 1489-1494 ◽  
Author(s):  
Michelle M. Duke ◽  
Andrew W. Hakin ◽  
Robert M. McKay ◽  
Kathryn E. Preuss
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Aqueous Solutions ◽  
Constant Pressure ◽  
Heat Capacities ◽  
Thermochemical Properties ◽  
Acid System ◽  
Standard State ◽  
Apparent Molar Heat Capacities ◽  
Fitting Procedures

Densities and volumetric heat capacities have been measured for aqueous solutions of L-valine, L-leucine, and L-isoleucine at 288.15, 298.15, 313.15, and 328.15 K. These data have been used to calculate apparent molar volumes, [Formula: see text] and apparent molar heat capacities, [Formula: see text] which in turn have been used to obtain standard state volumes, [Formula: see text] and standard state heat capacities, [Formula: see text] for each aqueous amino acid system. Helgeson, Kirkham, and Flowers equations, for neutral organics in water, have been used to model the calculated standard state volumes and heat capacities of the amino acids as a function of temperature at constant pressure. The results of our fitting procedures may be used to predict the behaviour of [Formula: see text] and [Formula: see text] for the selected amino acid systems outside of the temperature range utilised in this investigation.

Polyol–Water interactions. Apparent molal heat capacities and volumes of aqueous polyol solutions

1977 ◽  
Vol 55 (22) ◽  
pp. 3825-3830 ◽  
Author(s):  
Giuseppa DiPaola ◽  
Bernard Belleau
Keyword(s):  
Aqueous Solutions ◽  
Infinite Dilution ◽  
Pure Water ◽  
Water Environment ◽  
Heat Capacities ◽  
Flow Microcalorimeter ◽  
Specific Heats ◽  
Structural Interactions ◽  
Apparent Molal Heat Capacities

Volumetric specific heats (25 °C) and densities (24 °C) were measured with a flow microcalorimeter and flow densimeter for 12 polyols in water (0.05 to 2 m), and for NaCl and n-Bu4NBr in 1 m aqueous alditol solutions. The infinite dilution properties [Formula: see text] of the polyols show specificities in polyol−water interactions which are discussed in terms of the compatibility of the polyol stereochemistry and the existing water environment. The derived heat; capacities and volumes of transfer of hydrophobic and hydrophilic probes to aqueous solutions of homologous polyols suggest that structural interactions are reduced in these systems as compared to pure water.

Apparent Molal Volumes and Heat Capacities of Tetrabutylammonium Bromide in Aqueous Electrolyte Solutions

1975 ◽  
Vol 53 (21) ◽  
pp. 3206-3210 ◽  
Author(s):  
Nicole Desrosiers ◽  
Jacques E. Desnoyers
Keyword(s):  
Aqueous Solutions ◽  
Long Range ◽  
Transfer Functions ◽  
Aqueous Electrolyte ◽  
Tetrabutylammonium Bromide ◽  
Electrolyte Solutions ◽  
Heat Capacities ◽  
Apparent Molal Volumes ◽  
Flow Microcalorimeter ◽  
Molal Volumes

The apparent molal volumes and heat capacities of Bu4NBr were measured in aqueous solutions of NaF, NaCl, NaBr, KBr, NaAc, and NH4Ac at 25 °C with a flow densimeter and a flow microcalorimeter. The derived transfer functions of Bu4NBr from water to the electrolyte solutions, after correction for the long-range coulombic forces, are all negative. This suggests that the noncoulombic interactions between hydrophobic and hydrophilic ions result in negative contributions to volumes and heat capacities.

Structural characterization of folded and extended conformations in peptides containing γ amino acids with proteinogenic side chains: crystal structures of γn, (αγ)n and γγδγ sequences

2015 ◽  
Vol 39 (5) ◽  
pp. 3319-3326 ◽  
Author(s):  
Madhusudana M. B. Reddy ◽  
K. Basuroy ◽  
S. Chandrappa ◽  
B. Dinesh ◽  
B. Vasantha ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Crystal Structures ◽  
Structural Characterization ◽  
Side Chains ◽  
Amino Acid Residues

γn amino acid residues can be incorporated into structures in γn and hybrid sequences containing folded and extended α and δ residues.

Apparent molal heat capacities and volumes of aqueous electrolytes at 25 °C: NaClO3, NaClO4, NaNO3, NaBrO3, NaIO3, KClO3, KBrO3, KIO3, NH4NO3, NH4Cl, and NH4ClO4

1978 ◽  
Vol 56 (1) ◽  
pp. 24-28 ◽  
Author(s):  
Alain Roux ◽  
Goolam M. Musbally ◽  
Gérald Perron ◽  
Jacques E. Desnoyers ◽  
Prem Paul Singh ◽  
...  
Keyword(s):  
Aqueous Solutions ◽  
Infinite Dilution ◽  
Heat Capacities ◽  
Aqueous Electrolytes ◽  
Apparent Molal Volumes ◽  
Hückel Theory ◽  
Standard Values ◽  
Molal Volumes ◽  
Apparent Molal Heat Capacities

Measurements at 25 °C with flow calorimeters and densimeters have led to heat capacities and densities of aqueous solutions of 11 1:1 electrolytes: NaClO3, NaBrO3, NaIO3, NaNO3, NaClO4, NH4NO3, KClO3, KBrO3, KIO3, NH4Cl, and NH4ClO4. The first 6 salts were studied up to near saturation. We have used results of these measurements to obtain apparent molal heat capacities and apparent molal volumes of the various solutes. Extrapolation to infinite dilution on the basis of the Debye–Hückel theory bas led to [Formula: see text]and [Formula: see text] values for each solute. We have compared these standard values with results of earlier investigations.

Volumes and heat capacities of some amino acids in water at 25 °C

1977 ◽  
Vol 55 (19) ◽  
pp. 3364-3367 ◽  
Author(s):  
JagDish C. Ahluwalia ◽  
Claude Ostiguy ◽  
Gerald Perron ◽  
Jacques E. Desnoyers
Keyword(s):  
Amino Acids ◽  
Heat Capacities ◽  
Apparent Molal Volumes ◽  
Flow Microcalorimeter ◽  
Ionic Groups ◽  
The Poor ◽  
Molal Volumes

The apparent molal volumes and heat capacities of nine amino acids were measured in water at 25 °C with a flow densimeter and a flow microcalorimeter. It is shown that the poor additivity of the standard partial molal quantities of amino acids in water are attributable to the ionization of the two groups NH2 and COOH. The hydration of these ionic groups interfere with each other when they are separated by less than three carbon atoms.

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