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Effect of temperature on the partial molar volumes and the partial molar
compressibilities of α-amino acids in water and in aqueous solutions of strong
electrolytes

Article  in  Journal of Molecular Liquids · March 2017

DOI: 10.1016/j.molliq.2017.02.118

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Effect of temperature on the partial molar volumes and the partial molar

compressibilities of α-amino acids in water and in aqueous solutions of strong

electrolytes

Diana M. Rodrígueza, Carmen M. Romeroa1.

a
Departamento de Química, Universidad Nacional de Colombia. Bogotá, Colombia

Abstract

Density and sound velocity of glycine, alanine, α-aminobutyric acid, norvaline and

norleucine in water and in aqueous solutions of strong electrolytes have been determined in

the temperature range from 293.15 to 313.15 K at intervals of 5 K. The electrolytes used

are lithium chloride, sodium chloride, potassium chloride, ammonium sulfate and sodium

sulfate. The apparent molar volumes and the apparent molar compressibilities were

determined as a function of composition at each temperature from the experimental density

and sound velocity data. The limiting values of the partial molar volumes and the partial

molar adiabatic compressibilities at infinite dilution of the amino acids in water and in

aqueous electrolyte solutions were obtained at each temperature. The results confirm that

glycine and alanine behave as hydrophilic solutes while aminobutyric acid, norvaline and

norleucine exhibit a hydrophobic behavior and this behavior is also observed in the

presence of salts. The addition of electrolytes led to an increase of the partial molar

volumes and the partial molar compressibilities at infinite dilution suggesting that the

cations and anions of the salts interact directly with the zwitterionic group of the α-amino

1
Corresponding autor: Carmen M. Romero. E-mail:cmromeroi@unal.edu.co.
Departamento de Química, Universidad Nacional de Colombia. Calle 44 # 45-67 Bloque B9, Bogotá, Cód.
Postal 111311 - Colombia. Phone: 57 1 3165440. Fax (571) 3165220

1
acids, removing water molecules from hydration sphere of the amino acids, therefore

reducing their hydration number. The decrease of hydration number reflects a decrease of

electrostriction which leads to an increase of the partial molar properties. The results

suggest that the dehydrating ability of the salts used show a very good agreement with the

increase of the partial molar volume as well as the partial molar compressibility of the α-

amino acids.

Keywords: partial molar volume; partial molar compressibility; α-amino acids;

electrolytes; solute-solvent interactions.

1. Introduction

Amino acids are essential molecules for life: they are the constituent monomers of proteins,

and they are part of essential processes in organisms such as cell signaling and regulation of

gene expression.

-Amino acids in water adopt a zwitterionic form in which is the amine group is protonated

while the carboxyl group is deprotonated, thus the molecule has a zero net charge.

Therefore, amino acids can be considered as mixed solutes containing highly hydrophilic

groups (amine and carboxyl) and the hydrophobic aliphatic chain. These facts, combined

with their biological importance, make the study of the thermodynamic properties of these

compounds very interesting and relevant in aqueous solvents, where biological processes

occur. The presence of electrolytes has an important effect in the stability and behavior of

proteins in aqueous solutions and some authors assume that this is a consequence of their

2
interaction with the peptide groups. However, there is not a general and consistent

explanation about the behavior of these molecules in aqueous electrolyte solutions. [1–4].

Amino acids have been considered model compounds that provide useful information to

understand the behavior of proteins and the role of solvent structure in the stability of the

macromolecules. In fact, apparent molar volumes and the apparent molar compressibilities

of these compounds in water are very sensitive to solute-solvent interactions and thus they

have been used to provide an insight about hydration properties and solute-solvent

interactions[5–10]. Several studies have been reported on the volumes and compressibilities

of amino acids in aqueous electrolyte solutions [1,11–16], showing that the addition of salts

affects the interaction between the zwitterionic group and the water; in the case of strong

electrolytes, this is reflected in positive transfer volumes and compressibilities.

As a continuation of earlier works on the thermodynamic properties of amino acids in

aqueous solution [9,17–20], in the actual study we present the partial molar volumes and

the partial molar compressibilities of glycine, alanine, α-aminobutyric acid, norvaline and

norleucine in water and in aqueous solutions of lithium chloride, sodium chloride,

potassium chloride, ammonium sulfate and sodium sulfate at temperatures of (293.15,

298.15, 303.15, 308.15 and 313.15) K, this temperatures were selected since biological

systems are of special interest in our group research, therefore a small range of

temperatures close to the common body temperature is desired. The α-amino acids were

selected because they have a lineal hydrocarbon chain that increases its length by one

methylene group, as can be seen in Table 1, allowing the application of additivity

approaches to the partial molar volumes and the partial molar compressibilities at infinite

3
dilution. The electrolytes used are commonly found in living organisms, so the mixed

solvents used here could simulate the natural environment in which amino acids and other

biomolecules are present.

Most studies on the thermodynamic properties of amino acids in aqueous solutions have

been done on naturally occurring amino acids at 298.15 K, however, very few data are

reported in literature for amino acids such as norvaline and norleucine which have a linear

hydrocarbon chain, especially at temperatures different from 298.15 K [1,9,21]. In this

work, the influence of the temperature on the behavior of the partial molar properties of the

five α-amino acids in water and in aqueous solutions of the electrolytes has been used to

obtain information about the effect of the salts on solute hydration.

2. Materials and methods

2.1. Materials

The characteristics of the reagents used are presented in Table 1. The mass fraction purity is

reported according to the certificates of analysis. Amino acids and salts were used without

further purification. They were dried under vacuum at room temperature and kept in a

desiccator at least 48 h before use. Water was purified using a Barnstead Easy-Rodi DI

3321 system and degassed before use; the resulting water showed a conductivity less than

1.5 S·m-1 [22,23].

All solutions were prepared by weight using a Mettler balance AT-261 dual range with

readability of 1·10-5 g and reproducibility better than 1·10-4 g in the lower range. The

concentration of the electrolyte aqueous solutions used as solvents was the same; the

selected molality was 0.1500 mol·kg-1.

4
2.2. Methods

Densities and sound velocities of the aqueous solutions were measured using a vibrating U-

tube densimeter, Anton Paar DSA 5000, with a working frequency of 3 MHz and

temperature control better than 0.002 K, according to the manufacturer's specifications.

The densimeter was calibrated with dry air and purified water at 293.15 K. Density and

sound velocity reported data are the average of three independent measurements that were

reproducible within 1·10-3 kg·m-3 and 3·10-2 ms-1, respectively, with an uncertainty of

0.150 kg·m-3 for density and 2 ms-1 for sound velocity.

The apparent molar volumes V were calculated from the density experimental data using

equation (1):

( )
(1)

where M is the molar mass of the α-amino acid, m its molal concentration in the aqueous

solution, o is the density of the solvent (either pure water or electrolyte aqueous solution)

and is the solution density.

The apparent molar compressibilities, K, of the amino acid in water and in the aqueous

solutions of electrolytes were determined, respectively, from the density , and the

isentropic compressibility S, of the corresponding solution using the equation

(2)

5
where So is the isentropic compressibility of the solvent. The isentropic compressibilities

S of the aqueous solution at each temperature were calculated from both the sound speed,

u, and density measurements by means of the Newton-Laplace equation[24].

S = 1/ ρu2 (3)

The values of density and the isentropic compressibility of water at each temperature, used

in calibration were taken from the literature [25,26].

Experimental uncertainties were determined using the method described by Andraos [27].

The uncertainty of the molar properties at infinite dilution was assumed to be equal to those

of the most diluted solutions, which presented the biggest error in weighing.

3. Results and discussion

Data for density , sound velocity u, apparent molar volumes and apparent molar

compressibilities at temperatures of (293.15, 298.15, 303.15, 308.15 and 313.15) K of

the amino acids in water and in the mixed solvents is presented in the supporting material

of this paper. The values obtained in this work for the properties of the aqueous solutions

of electrolytes used as mixed solvents, are in good agreement with previously published

values [14,28–31].

3.1 Partial Molar Volumes

The dependence of the apparent molar volumes of the α-amino acids with the molality at

the selected temperatures was fitted by a least squares method to a second order polynomial

equation. The value for the apparent molar volume at infinite dilution, which is equal to the

partial molar one, ̅ , was obtained by extrapolation. In all cases the apparent molar

6
volume of the α-amino acids in water and in the mixed solvents increases with the

concentration.

Table 2 shows the partial molar volumes at infinite dilution of the α-amino acids at the

selected temperatures; as can be seen, good agreement is found between the results

obtained in this work and the values reported in literature. The apparent molar volumes of

the α-amino acids in electrolyte aqueous solutions as a function of molality were adjusted

using the least squares method to second order polynomial equation; the values of the

partial molar volume at infinite dilution obtained by extrapolation are presented in Tables 3

– 7 as well as the partial molar volumes of transfer, defined by Equation 4.

̅ ̅ ̅ (4)

Where, ̅ is the partial molar volume of the amino acid in the mixed solvent, and

̅ is the partial molar volume of the amino acid in water ̅ is the partial molar

volume of transfer.

Figure 1 shows the partial molar volume of glycine in water and in the salt solutions at the

five temperatures of study. It is clear that in all the mixed solvents the value of ̅ is larger

than the result in obtained in water and this behavior is the same for all five α-amino acids.

According to the co-sphere overlap model [32], the interaction between two ions results in

positive values of ̅ , while interactions between a hydrophobic group and an ion give

negative ̅ . Tables 3 – 7 show that in all cases the addition of salts yields positive

values of partial molar volumes of transfer, indicating that the interaction between the

zwitterionic group of the amino acids and the hydrated cations and anions of the salts is

7
predominant. Moreover, it is observed that for all five α- amino acids, the effect of the salt

over the partial molar volumes follows the order indicated below:

̅ LiCl < ̅ KCl < ̅ NaCl < ̅ (NH4)2SO4 < ̅ Na2SO4

The observed trend is related with the Hofmeister’s series, which is an empiric organization

of the ability of the ions to stabilize proteins[33]. It has been found that strongly hydrated

anions (such as PO42- and SO42-) and weakly hydrated cations (Ca2+ and Al3+) have a

stabilizing effect since they attract water molecules from the hydration sphere of the protein

to hydrate themselves, minimizing the hydrophobic interaction. Knowing that amino acids

are the constituents units of proteins, it is expected that the same dehydration ability of the

ions take place in the systems of this study; thus it could be |proposed that the presence of

the salts in solution leads to loose water from the hydration sphere of the amino acids,

decreasing the electrostriction and therefore increasing the partial molar volume of the

solutes.

In order to analyze if the partial molar volume at infinite dilution can be described in terms

of group contributions according to a methylene additivity approach based on the

dependence of the property on the number of carbon atoms or the number of methylene

groups, the partial molar volume at infinite dilution of the amino acids in water and in the

mixed solvents was represented by the following equation:

V20  V20 ( NH3 , COO )  nV20 (CH 2 ) (5)

Where n represents the number of methylene groups, V20 (CH 2 ) and V20 ( NH3 , COO ) are

the volumetric contributions of the methylene, and the amino and carboxylic groups to the

partial molar volume of the amino acid; the contribution of the methylene group comprises

8
also the contribution for the hydrogen atom at the end of alkyl. According to Hakin, the

number of carbon atoms is approximately equivalent to the number of methylene groups

[6,8,34].

The dependence of the partial molar volumes at infinite dilution with the number of

methylene groups is well represented by linear equations with the form of equation (5). The

group contributions of the methylene and the polar groups are listed in Table 8. As the

temperature becomes larger the volumetric contributions ̅ and ̅

increase; the values of the methylene group contribution in water at 298.15 K determined in

this work (15.98 cm3 mol-1) agree well with other authors like Millero (15.90 cm3 mol-1)[6]

and Mallick (16.11 cm3 mol-1)[35].

It is very interesting that the contribution of the methylene group is smaller in the mixed

solvents than in water and it is almost the same no matter the nature of the salt used as co-

solute. On the other hand, the polar group contribution is significantly larger in the presence

of the electrolytes and the same trend found with the partial molar volumes of transfer is

observed with this contribution. This fact enhances the previous observation that the

interaction between the zwitterionic group and the ions is dominant over the hydrophobic

interaction and that the ion-ion interaction dehydrates the α-amino acid depending on the

hydration of the cations and anions of the electrolytes.

The partial molar expansibility (Equation 6) of the α-amino acids in water and in the mixed

solvents was calculated and the values obtained are shown in Table 9.

̅
̅ (6)

9
The dependence of the partial molar volumes of the amino acids in both water and in the

mixed solvents is linear, which is probably a result of the narrow range of temperatures of

the study; therefore, the partial molar expansibilities obtained are constant showing that for

the systems considered they do not depend on temperature. It can be seen that there are no

significant changes in the values of ̅ due to the addition of salts, which led us to

conclude that the concentration of the electrolytes is no enough to shift the relationship

between the partial molar volume and the temperature.

3.2 Partial molar compressibility

The dependence of the apparent molar compressibilities of the α-amino acids with molality

was fitted at all temperatures by a least squares method to second order polynomial

equation. The partial molar compressibilities at infinite dilution ̅ obtained by

extrapolation are shown in Table 10.

The partial molar compressibilities of the amino acids in water at all temperatures are

negative and become larger as the number of methylene groups of the non-polar chain of

the amino acid increases. Table 11 shows comparison between our data and the data

reported by other authors at 298.15 K.

The compressibilities at infinite dilution become less negative as the temperature increases.

The dependence of the partial molar compressibilities of the α-amino acids with

temperature is well represented by a second order polynomial equation (Equation 7),

indicating that ̅ is more sensitive to the changes of temperature than ̅ , since ̅ ⁄

depends on temperature while ̅ is a constant.

10
̅ (7)

In order to study the effect of temperature, we plotted ̅ ⁄ and ̅ as functions of the

number of methylene groups as shown in Figure 2. Until 303.15 K these curves have

similar shapes with a minimum in alanine. This results are pretty alike to those found by

Chalikian[36] for α,ω-amino acids which show a minimum for γ-amino butyric acid. The

data found confirm the previous discussion about the hydrophilic behavior of glycine and

alanine, since the change of the partial molar compressibility due to temperature ̅ ⁄

and ̅ ⁄ decreases as the carbon chain increases, while for AABA, norvaline and

norleucine as the number of methylene groups become larger, an increase of the values of

̅ ⁄ y ̅ ⁄ , is observed, indicating the importance of hydrophobic interactions. In

the case of (308.15 and 313.15) K, the minimum moves from alanine to AABA, which

could mean that the contribution of hydrophilic group becomes larger as the temperature

increase, however we don’t have an explanation for this result.

Tables 12 – 16 show the partial molar compressibilities at infinite dilution of the α-amino

acids in the mixed solvents, as well as the partial molar compressibilities of transfer,

defined by Equation 8.

̅ ̅ ̅ (8)

Where ̅ is the partial molar compressibility of transfer, ̅ is the partial molar

compressibility of the amino acid in the mixed solvent, and ̅ is the partial molar

compressibility of the amino acid in water.

11
In all cases the partial molar compressibilities of transfer are positive as expected since the

electrostriction decreases, leading to a rise of the partial molar volume producing an

increase of the partial molar compressibilities of the amino acids. The highest effect on the

partial molar compressibilities of transfer is due to Na2SO4 and the effect of the salts can be

represented in the following way:

̅ LiCl < ̅ KCl < ̅ NaCl < ̅ (NH4)2SO4 < ̅ Na2SO4

The trend follows the same behavior observed for the partial molar volumes of transfer.

The hydration numbers, nH, of the amino acids in water and in the mixed solvents, were

determined using the model proposed by Millero [6] and they are presented in Table 16.

According to the model, the partial molar volume of an amino acid ̅ can be obtained

using Equation 9.

̅ ̅ ̅ (9)

Where ̅ is the intrinsic partial molar volume of the amino acid and ̅ is the

electrostriction partial molar volume due to the hydration of the amino acid. The decrease

in volume due to electrostriction can be related to the number of water molecules (nH)

hydrated to the amino acid:

̅ ̅ ̅ (10)

̅ is the molar volume of electrostricted water and ̅ is the molar volume of bulk water.

The hydration numbers, nH is determined from equation 11:

̅
̅
(11)

12
Where is the isentropic compressibility of the solvent (Equation 3) and ̅ is the molar

volume of water, taken from literature[37].

The results presented in Table 17 reflect the dehydration of the α-amino acids due to the

addition of salts; these results explain the positive values of ̅ and ̅ . In all cases

and at all temperatures it was found that:

nH Water > nH LiCl > nH NaCl > nH KCl > nH (NH4)2SO4 > nH Na2SO4

This is in agreement with the trend found for the effect of salts on partial molar volumes

and partial molar compressibilities at infinite dilution.

4. Conclusions

Partial molar volumes and partial molar compressibilities at infinite dilutions were

determined for glycine, alanine, aminobutyric acid, norvaline and norleucine in water and

in aqueous solutions of electrolytes in the temperature range from 293.15 to 313.15 K.

From the behavior in water, we conclude that glycine and alanine are hydrophilic solutes,

while interactions between AABA, norvaline and norleucine and water are mainly

hydrophobic.

The addition of salts produces an increase in the partial molar volumes and

compressibilities of the α-amino acids, which suggests that the interaction between the

zwitterionic group and the anions and cations of the salt is predominant. This interaction

between ions leads to removal of water molecules from the hydration sphere of the amino

acids to the bulk, reducing the electrostriction which increases the partial molar properties

of the solutes.

13
Using the hydration number of the α-amino acids in water and in the mixed solvent, it can

be concluded that the dehydrating ability of anions and cations constituting the salts is

directly related to the partial molar volumes and compressibilities of transfer, allowing to

order the electrolytes according to their effect on the properties of the amino acids and to

relate it to the Hofmeister’s series.

5. Acknowledgements

This work was supported by the Universidad Nacional de Colombia and the Instituto

Colombiano para el Desarrollo de la Ciencia y la Tecnología. Francisco José de Caldas.

COLCIENCIAS. through the YOUNG RESEARCHERS NATIONAL PROGRAM and the

Universidad Nacional de Colombia grants DIB: 23605 and 046 – 2015 COLCIENCIAS.

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Some Amino Acids in Aqueous Sodium Acetate Solutions at 298.15 K, J. Chem. Eng.
Data. 49 (2004) 1236–1246.

[42] H.D. Ellerton, G. Reinfelds, D.E. Mulcahy, P.J. Dunlop, Activity, Density, and
Relative Viscosity Data for Several Amino Acids, Lactamide, and Raffinose in
Aqueous Solution at 25°, J. Phys. Chem. 68 (1964) 398–402.

[43] M. Kikuchi, M. Sakurai, K. Nitta, Partial Molar Volumes and Adiabatic

Compressibilities of Amino Acids in Dilute Aqueous Solutions at 5, 15, 25, 35, and
45ºC, J. Chem. Eng. Data. 40 (1995) 935–942.

[44] R.K. Wadi, R.K. Goyal, Densities, viscosities, and application of transition-state
theory for water + potassium thiocyanate + amino acid solutions at 288.15-308.15 K,
J. Chem. Eng. Data. 37 (1992) 377–386.

[45] R. Wadi, R. Goyal, Temperature dependence of apparent molar volumes and viscosity
B-coefficients of amino acids in aqueous potassium thiocyanate solutions from 15 to
35°C, J. Solution. Chem. 21 (1992) 163–170.

[46] E. Berlin, M.J. Pallansch, Densities of several proteins and L-amino acids in the dry
state, J. Phys. Chem. 72 (1968) 1887–1889.

18
Table 1: Sample description

Purity (mass
Name Chemical Structure Source CAS Number
fraction)

Glycine Aldrich 56-40-6 >0.98

Alanine Sigma 56-41-7 >0.99

AABA Aldrich 2835-81-6 >0.99

Norvaline Sigma 760-78-1 >0.99

Norleucine Sigma 327-57-1 >0.99

Lithium chloride
LiCl Sigma 7447-41-1 >0.99
Sodium chloride
NaCl Merck 7647-14-5 >0.995
Potassium chloride
KCl Merck 7447-40-7 >0.995
Ammonium sulfate
(NH4)2SO4 Carlo Erba 7783-20-2 0.99
Sodium sulfate
Na2SO4 Merck 7757-82-6 0.99

19
Table 2: Partial molar volumes of α-amino acids in water from T = 293.15 to 313.15 K at
75 kPa.

̅ /
T/K
Glycine Literature Alanine Literature AABA Literature
293.15 42.90 42.8[38] 60.03 60.01[39] 74.98 74.98[9]
298.15 43.33 43.3[5] 43.33[40] 60.38 60.41[41] 60.43[6] 75.56 75.64[9]75.62[42]
303.15 43.86 43.89[39] 60.72 60.63[39] 75.92 75.89[9]
308.15 44.31 44.2[10] 61.00 60.96[43] 76.40 76.20[10]
313.15 44.63 44.52[39] 61.35 61.20[5] 77.00 77.40[7]
̅ /
T/K
Norvaline Literature Norleucine Literature
293.15 91.06 91.03[9] 106.89 106.88[9]
298.15 91.74 91.77 [9] 91.70[7] 107.56 107.58[9] 107.60[5]
303.15 92.26 92.21[9] 108.25 108.22[9]
308.15 92.76 92.68[21] 108.84 108.16[21]
313.15 93.51 -- 109.58 109.20[5]

a. (̅ ) obtained by extrapolation from the apparent molar volumes as a function of molality

b. u(P) = 1 kPa
c. u(T) = 0.01 K

20
Table 3: Partial molar volumes at infinite dilution of α-amino acids in aqueous lithium
chloride 0.1500 m and partial molar volumes of transfer from water to the aqueous
electrolyte solution from T = 293.15 to 313.15 K at 75 kPa.

Glycine Alanine AABA

T/K ̅ / ̅ / ̅ / ̅ / ̅ / ̅ /

293.15 43.19 0.29 60.25 0.23 75.15 0.17

298.15 43.64 0.31 60.63 0.26 75.74 0.20
303.15 44.17 0.30 60.98 0.27 76.11 0.19
308.15 44.57 0.31 61.25 0.26 76.58 0.19
313.15 44.95 0.31 61.58 0.25 77.20 0.20

Norvaline Norleucine
T/K ̅ / ̅ / ̅ / ̅ /

293.15 91.21 0.16 107.00 0.12

298.15 91.90 0.16 107.67 0.10
303.15 92.42 0.17 108.39 0.13
308.15 92.92 0.16 108.96 0.12
313.15 93.71 0.19 109.62 0.03

a. (̅ ) obtained by extrapolation from the apparent molar volumes as a function of molality

b. u(P) = 1 kPa
c. u(T) = 0.01 K
d. u(m salt) = 1·10-4 mol·kg-1

21
Table 4: Partial molar volumes at infinite dilution of α-amino acids in aqueous sodium
chloride 0.1500 m and partial molar volumes of transfer from water to the aqueous
electrolyte solution from T = 293.15 to 313.15 K at 75 kPa.

Glycine Alanine AABA

T/K ̅ / ̅ / ̅ / ̅ / ̅ / ̅ /

293.15 43.36 0.46 60.40 0.38 75.31 0.33

298.15 43.78 0.45 60.75 0.38 75.88 0.34
303.15 44.31 0.44 61.08 0.37 76.25 0.33
308.15 44.71 0.45 61.35 0.36 76.72 0.33
313.15 45.08 0.44 61.70 0.37 77.32 0.32

Norvaline Norleucine
T/K ̅ / ̅ / ̅ / ̅ /

293.15 91.35 0.30 107.16 0.28

298.15 92.05 0.31 107.83 0.26
303.15 92.56 0.31 108.56 0.30
308.15 93.06 0.30 109.13 0.29
313.15 93.82 0.30 109.86 0.27

a. (̅ ) obtained by extrapolation from the apparent molar volumes as a function of molality

b. u(P) = 1 kPa
c. u(T) = 0.01 K
d. u(m salt) = 1·10-4 mol·kg-1

22
Table 5: Partial molar volumes at infinite dilution of α-amino acids in aqueous potassium
chloride 0.1500 m and partial molar volumes of transfer from water to the aqueous
electrolyte solution from T = 293.15 to 313.15 K at 75 kPa.

Glycine Alanine AABA

T/K ̅ / ̅ / ̅ / ̅ / ̅ / ̅ /

293.15 43.27 0.37 60.33 0.31 75.24 0.26

298.15 43.68 0.35 60.67 0.30 75.80 0.26
303.15 44.25 0.38 61.00 0.29 76.17 0.25
308.15 44.61 0.35 61.29 0.30 76.64 0.25
313.15 45.01 0.37 61.63 0.30 77.26 0.26

Norvaline Norleucine
T/K ̅ / ̅ / ̅ / ̅ /

293.15 91.29 0.24 107.10 0.22

298.15 91.97 0.23 107.76 0.19
303.15 92.48 0.23 108.47 0.21
308.15 92.98 0.22 109.05 0.21
313.15 93.78 0.26 109.80 0.21

a. (̅ ) obtained by extrapolation from the apparent molar volumes as a function of molality

b. u(P) = 1 kPa
c. u(T) = 0.01 K
d. u(m salt) = 1·10-4 mol·kg-1

23
Table 6: Partial molar volumes at infinite dilution of α-amino acids in aqueous ammonium
sulfate 0.1500 m and partial molar volumes of transfer from water to the aqueous
electrolyte solution from T = 293.15 to 313.15 K at 75 kPa.

Glycine Alanine AABA

T/K ̅ / ̅ / ̅ / ̅ / ̅ / ̅ /

293.15 43.71 0.81 60.74 0.72 75.65 0.67

298.15 44.13 0.80 61.10 0.73 76.23 0.69
303.15 44.71 0.84 61.43 0.72 76.58 0.66
308.15 45.09 0.83 61.70 0.71 77.06 0.67
313.15 45.50 0.86 62.07 0.74 77.68 0.68

Norvaline Norleucine
T/K ̅ / ̅ / ̅ / ̅ /

293.15 91.69 0.64 107.50 0.62

298.15 92.38 0.64 108.18 0.61
303.15 92.89 0.64 108.89 0.63
308.15 93.38 0.62 109.43 0.59
313.15 94.14 0.62 110.19 0.60

a. (̅ ) obtained by extrapolation from the apparent molar volumes as a function of molality

b. u(P) = 1 kPa
c. u(T) = 0.01 K
d. u(m salt) = 1·10-4 mol·kg-1

24
Table 7: Partial molar volumes at infinite dilution of α-amino acids in aqueous sodium
sulfate 0.1500 m and partial molar volumes of transfer from water to the aqueous
electrolyte solution from T = 293.15 to 313.15 K at 75 kPa.

Glycine Alanine AABA

T/K ̅ / ̅ / ̅ / ̅ / ̅ / ̅ /

293.15 44.01 1.11 61.04 1.02 75.94 0.96

298.15 44.43 1.10 61.40 1.03 76.53 0.99
303.15 45.01 1.14 61.72 1.01 76.88 0.96
308.15 45.39 1.13 62.00 1.01 77.36 0.97
313.15 45.80 1.16 62.36 1.03 77.97 0.97

Norvaline Norleucine
T/K ̅ / ̅ / ̅ / ̅ /

293.15 91.99 0.94 107.78 0.90

298.15 92.68 0.94 108.46 0.89
303.15 93.19 0.94 109.17 0.91
308.15 93.68 0.92 109.72 0.88
313.15 94.43 0.91 110.47 0.88

a. (̅ ) obtained by extrapolation from the apparent molar volumes as a function of molality

b. u(P) = 1 kPa
c. u(T) = 0.01 K
d. u(m salt) = 1·10-4 mol·kg-1

25
Table 8: Group contributions to the partial molar volume of the α-amino acids in water and
in the aqueous electrolyte solution from T = 293.15 to 313.15 K at 75 kPa.

Water LiCl 0.1500 m NaCl 0.1500 m

̅ ̅
T/K ̅ ̅ / ̅ / ̅
/ /
/ /
293.15 15.90 27.47 15.86 27.79 15.86 27.95
298.15 15.98 27.77 15.93 28.12 15.94 28.24
303.15 16.03 28.11 15.99 28.45 16.00 28.56
308.15 16.08 28.41 16.05 28.72 16.06 28.83
313.15 16.21 28.59 16.15 28.97 16.17 29.05
KCl 0.1500 m (NH4)2SO4 0.1500 m Na2SO4 0.1500 m
T/K ̅ / ̅ ̅ / ̅ ̅ / ̅
/ / /
293.15 15.86 27.86 15.85 28.30 15.85 28.61
298.15 15.95 28.14 15.94 28.59 15.93 28.90
303.15 15.99 28.50 15.98 28.95 15.98 29.26
308.15 16.06 28.74 16.04 29.22 16.03 29.53
313.15 16.17 28.98 16.15 29.48 16.14 29.78

a. u(̅ ) = 0.17 cm3 mol-1 (max)

b. u(̅ ) = 0.56 cm3 mol-1 (max)
a. u(m salt) = 1·10-4 mol·kg-1
c. u(P) = 1 kPa
d. u(T) = 0.01 K

26
Table 9: Partial molar expansibility of α-amino acids in water and in the aqueous
electrolyte solution from T = 293.15 to 313.15 K at 75 kPa.

̅ /
Amino acid LiCl NaCl KCl (NH4)2SO4 Na2SO4
Water
0.1500 m 0.1500 m 0.1500 m 0.1500 m 0.1500 m
Glycine 8.8 8.9 8.7 8.8 9.0 9.1
Alanine 6.5 6.5 6.4 6.4 6.5 6.5
AABA 9.8 9.8 9.7 9.8 9.7 9.8
Norvaline 12.0 12.0 11.9 12.0 11.8 11.8
Norleucine 13.0 13.0 13.4 13.4 13.2 13.3

a. u( ̅ ) = 0.6 cm3 mol-1 K-1 (max)

b. u(P) = 1 kPa
c. u(T) = 0.01 K
d. u(m salt) = 1·10-4 mol·kg-1

27
Table 10: Partial molar compressibilities at infinite dilution of the α-amino acids in water
from T = 293.15 to 313.15 K at 75 kPa.

̅ /
T/K
Glycine Alanine AABA Norvaline Norleucine
293.15 28.49 29.53 31.67 34.75 38.34
298.15 25.10 25.93 26.56 30.03 34.52
303.15 22.80 23.85 24.44 25.72 28.31
308.15 19.20 20.26 21.74 22.97 24.62
313.15 16.78 17.97 18.82 19.63 22.46

a. ( ̅ ) obtained by extrapolation from the apparent molar volumes as a function of molality

b. u(P) = 1 kPa
c. u(T) = 0.01 K

28
Table 11: Literature comparison of the partial molar compressibilities at infinite dilution of
the α-amino acids in water at 298.15 K.

̅ /
α-amino acid This work Literature
Glycine 25.10 25.97[6] 26.6[34] 24.09[44] 27.16[44] 26.40[43]
Alanine 25.93 25.56[6] 25.1[34] 26.28[45] 24.74[44] 25.16[43]
AABA 26.56 27.1[34] 29.95[46]
Norvaline 30.03 29.0[34]29.70[46]
Norleucine 34.52 30.3[34]

a. ( ̅ ) obtained by extrapolation from the apparent molar volumes as a function of molality

b. u(T) = 0.01 K

29
Table 12: Partial molar compressibilities at infinite dilution and partial molar
compressibilities of transfer of the α-amino acids in aqueous lithium chloride 0.1500 m
from T = 293.15 to 313.15 K at 75 kPa.

Glycine Alanine AABA

T/K ̅ / ̅ / ̅ / ̅ / ̅ / ̅ /

293.15 27.32 1.17 27.34 2.19 29.76 1.91

298.15 23.32 1.78 24.47 1.46 24.77 1.79
303.15 21.22 1.58 21.83 2.02 22.53 1.91
308.15 17.12 2.08 18.43 1.83 20.12 1.62
313.15 15.61 1.17 16.32 1.65 17.40 1.42

Norvaline Norleucine
T/K ̅ / ̅ / - ̅ / ̅ /

293.15 32.61 2.14 36.68 1.66

298.15 28.14 1.89 32.59 1.93
303.15 23.46 2.26 26.63 1.68
308.15 20.34 2.63 22.09 2.53
313.15 17.66 1.97 20.02 2.44

a. ( ̅ ) obtained by extrapolation from the apparent molar volumes as a function of molality

b. u(P) = 1 kPa
c. u(T) = 0.01 K
d. u(m salt) = 1·10-4 mol·kg-1

30
Table 13: Partial molar compressibilities at infinite dilution and partial molar
compressibilities of transfer of the α-amino acids in aqueous sodium chloride 0.1500 m
from T = 293.15 to 313.15 K at 75 kPa.

Glycine Alanine AABA

T/K ̅ / ̅ / ̅ / ̅ / ̅ / ̅ /

293.15 25.02 3.47 25.62 3.91 28.08 3.59

298.15 21.70 3.40 22.76 3.17 22.13 4.43
303.15 19.71 3.09 19.29 4.56 20.69 3.75
308.15 15.67 3.53 17.05 3.21 18.21 3.53
313.15 14.07 2.71 14.25 3.72 15.05 3.77

Norvaline Norleucine
T/K ̅ / ̅ / ̅ / ̅ /

293.15 30.72 4.03 34.28 4.06

298.15 26.24 3.79 30.22 4.30
303.15 21.66 4.06 24.21 4.10
308.15 18.49 4.48 20.95 3.67
313.15 15.88 3.75 18.73 3.73

a. ( ̅ ) obtained by extrapolation from the apparent molar volumes as a function of molality

b. u(P) = 1 kPa
c. u(T) = 0.01 K
d. u(m salt) = 1·10-4 mol·kg-1

31
Table 14: Partial molar compressibilities at infinite dilution and partial molar
compressibilities of transfer of the α-amino acids in aqueous potassium chloride 0.1500 m
from T = 293.15 to 313.15 K at 75 kPa.

Glycine Alanine AABA

T/K ̅ / ̅ / ̅ / ̅ / ̅ / ̅ /

293.15 25.71 2.78 26.33 3.20 28.62 3.05

298.15 22.39 2.71 22.99 2.94 23.26 3.30
303.15 20.26 2.54 20.46 3.39 21.27 3.17
308.15 16.42 2.78 17.62 2.64 18.75 2.99
313.15 14.64 2.14 14.88 3.09 15.77 3.05

Norvaline Norleucine
T/K ̅ / ̅ / ̅ / ̅ /

293.15 31.34 3.41 35.47 2.87

298.15 27.02 3.01 31.39 3.13
303.15 22.36 3.36 25.43 2.88
308.15 19.24 3.73 21.24 3.38
313.15 16.58 3.05 19.14 3.32

a. ( ̅ ) obtained by extrapolation from the apparent molar volumes as a function of molality

b. u(P) = 1 kPa
c. u(T) = 0.01 K
d. u(m salt) = 1·10-4 mol·kg-1

32
Table 15: Partial molar compressibilities at infinite dilution and partial molar
compressibilities of transfer of the α-amino acids in aqueous ammonium sulfate 0.1500 m
from T = 293.15 to 313.15 K at 75 kPa.

Glycine Alanine AABA

T/K ̅ / ̅ / ̅ / ̅ / ̅ / ̅ /

293.15 23.75 4.74 24.41 5.12 27.25 4.42

298.15 20.56 4.54 21.52 4.41 21.84 4.72
303.15 18.56 4.24 18.56 5.29 19.89 4.55
308.15 14.71 4.49 16.39 3.87 17.50 4.24
313.15 13.16 3.62 13.74 4.23 14.60 4.22

Norvaline Norleucine
T/K ̅ / ̅ / ̅ / ̅ /

293.15 29.73 5.02 33.42 4.92

298.15 25.37 4.66 29.51 5.01
303.15 20.87 4.85 23.78 4.53
308.15 17.85 5.12 20.58 4.04
313.15 15.41 4.22 18.46 4.00

a. ( ̅ ) obtained by extrapolation from the apparent molar volumes as a function of molality

b. u(P) = 1 kPa
c. u(T) = 0.01 K
d. u(m salt) = 1·10-4 mol·kg-1

33
Table 16: Partial molar compressibilities at infinite dilution and partial molar
compressibilities of transfer of the α-amino acids in aqueous sodium sulfate 0.1500 m from
T = 293.15 to 313.15 K at 75 kPa.

Glycine Alanine AABA

T/K ̅ / ̅ / ̅ / ̅ / ̅ / ̅ /

293.15 21.50 6.99 22.37 7.16 24.63 7.04

298.15 18.41 6.69 19.77 6.16 21.15 5.41
303.15 13.79 9.01 14.74 9.11 16.00 8.44
308.15 12.28 6.92 13.75 6.51 15.98 5.76
313.15 10.33 6.45 11.72 6.25 13.04 5.78

Norvaline Norleucine
T/K ̅ / ̅ / ̅ / ̅ /

293.15 27.37 7.38 30.41 7.93

298.15 23.23 6.80 24.61 9.91
303.15 17.25 8.47 18.94 9.37
308.15 16.01 6.96 17.00 7.62
313.15 14.08 5.55 15.12 7.34

a. ( ̅ ) obtained by extrapolation from the apparent molar volumes as a function of molality

b. u(P) = 1 kPa
c. u(T) = 0.01 K
d. u(m salt) = 1·10-4 mol·kg-1

34
Table 17: Hydration numbers of the α-amino acids in water and in the aqueous electrolyte
solution from T = 293.15 to 313.15 K at 75 kPa.

nH (Water)
T/K
Glycine Alanine AABA Norvaline Norleucine
293.15 3.46 3.59 3.85 4.22 4.66
298.15 3.10 3.20 3.28 3.71 4.27
303.15 2.86 2.99 3.06 3.22 3.55
308.15 2.43 2.57 2.75 2.91 3.12
313.15 2.14 2.30 2.40 2.51 2.87
nH (LiCl 0.1500 m)
T/K
Glycine Alanine AABA Norvaline Norleucine
293.15 3.37 3.38 3.68 4.03 4.53
298.15 2.93 3.07 3.11 3.53 4.09
303.15 2.70 2.78 2.87 2.98 3.39
308.15 2.20 2.37 2.59 2.61 2.84
313.15 2.02 2.11 2.25 2.29 2.59
nH (NaCl 0.1500 m)
T/K
Glycine Alanine AABA Norvaline Norleucine
293.15 3.10 3.18 3.48 3.81 4.25
298.15 2.73 2.87 2.79 3.31 3.81
303.15 2.52 2.46 2.64 2.76 3.09
308.15 2.02 2.20 2.35 2.38 2.70
313.15 1.83 1.85 1.96 2.06 2.43
nH (KCl 0.1500 m)
T/K
Glycine Alanine AABA Norvaline Norleucine
293.15 3.18 3.26 3.55 3.88 4.39
298.15 2.82 2.89 2.93 3.40 3.95
303.15 2.58 2.61 2.71 2.85 3.24
308.15 2.12 2.27 2.42 2.48 2.74
313.15 1.90 1.93 2.05 2.15 2.49
nH ((NH4)2SO4 0.1500 m)
T/K
Glycine Alanine AABA Norvaline Norleucine
293.15 3.00 3.08 3.44 3.75 4.22
298.15 2.64 2.76 2.80 3.25 3.78
303.15 2.41 2.41 2.58 2.71 3.09
308.15 1.93 2.15 2.30 2.34 2.70
313.15 1.74 1.82 1.93 2.04 2.44
nH (Na2SO4 0.1500 m)
T/K
Glycine Alanine AABA Norvaline Norleucine
293.15 2.75 2.87 3.15 3.51 3.90
298.15 2.39 2.57 2.75 3.02 3.20
303.15 1.82 1.94 2.11 2.27 2.49
308.15 1.63 1.83 2.12 2.13 2.26
313.15 1.38 1.57 1.75 1.89 2.02
a. u(nH) = 0.64 (max)
b. u(P) = 1 kPa
c. u(T) = 0.01 K
d. u(m salt) = 1·10-4 mol·kg-1

35
 46.00

45.50

45.00

44.50

44.00

43.50

43.00

42.50
290.00 295.00 300.00 305.00 310.00 315.00
T/K

Figure 1: Partial molar volumes at infinite dilution of glycine in water and in the aqueous
electrolyte solution at different temperatures.

36
 14.00 A
13.00
12.00
11.00
10.00
9.00
8.00
7.00
6.00
0 1 2 3 4 5 6
-CH₂

1.250E-04 B
𝟏
𝑲

1.150E-04
𝟏
𝑮𝑷𝒂

1.050E-04
9.500E-05
𝟏

8.500E-05
̅ 𝟐 ⁄𝝏𝑻 /𝒄𝒎𝟑 𝒎𝒐𝒍

7.500E-05
6.500E-05
5.500E-05
4.500E-05
𝝏𝑲

3.500E-05
0 1 2 3 4 5 6
-CH₂

Figure 2: (A) Partial molar expansibilities of the α-amino acids as a function of the
methylene groups. (B) ̅ ⁄ of the α-amino acids as a function of the methylene
groups.

37

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