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Investigations of Various Amino acids in different Aqueous Solutions of Potassium Nitrate at Various Temperatures in
terms of Partial Molar Volumes
II. EXPERIMENTAL SECTION DL--alanine 0.28 0.58 0.90 1.67 1.97 2.47
The amino acids selected for the present study glycine
(G-7126), DL--alanine (A-7502), DL--amino-n-butyric 0.04 0.04 0.06 0.04 0.04 0.10
acid (A-1754), L-valine (V-0500) and L-leucine (L-8000) DL--amino-n-butyric 0.54 0.80 1.06 1.40 2.06 2.43
were obtained from sigma chemicals co. these along with acid
potassium nitrate (AR, S.d. fine chemicals Ltd., India), were 0.04 0.04 0.04 0.04 0.05 0.04
used without further purification and dried over anhydrous L-valine 0.14 0.27 0.58 0.75 1.10 1.47
CaCl2 in a vacuum desiccator before use. Deionized, doubly
distilled degassed water with a specific conductance of less 0.03 0.04 0.03 0.03 0.07 0.04
than 1.3 10-4 m-1 was used for all of the measurements. All L-leucine 0.43 0.56 0.65 0.80 1.14 1.62
solutions were prepared by mass using a mettler balance with
an accuracy of 0.01 mg. 0.06 0.05 0.04 0.04 0.06 0.07
The solution densities were measured using a vibrating tube T= 308.15 K
digital densimeter (model DMA 60/602, Anton paar), with
Glycine 0.29 0.37 1.08 1.72 2.04 2.55
precision of 110-3 kgm-3 accuracy of 310-3 kgm-3.
Densities function was checked by measuring the densities of
0.08 0.06 0.09 0.12 0.09 0.09
aqueous sodium chloride solutions, which agreed well with
the literature values[Millero et al. (1978][literature values of DL--alanine 0.19 0.42 0.74 1.14 2.01 2.25
density are: (1005.571, 1017.344, 1036.690, 1054.672,
0.18 0.14 0.14 0.13 0.18 0.24
1071.353 and 1087.608) kgm-3 at 0.20918, 0.50653,
`
1.01279, 1.50262, 1.97403, and 2.44952) molkg-1of sodium
chloride, respectively] at 298.15 K. The temperature of water DL--amino-n-butyric 0.19 0.27 0.45 0.98 1.47 2.19
around the densimeter cell was controlled to within 0.01K. acid
0.14 0.13 0.13 0.13 0.14 0.16
L-valine 0.02 0.34 0.36 0.87 1.03 2.0
III. RESULTS AND DISCUSSION
0.08 0.11 0.12 0.08 0.08 0.13
The standard partial molar volumes,V2,of amino acids in
L-leucine 0.16 0.25 0.29 0.80 1.16 1.77
water and ion aqueous potassium nitrate solutions of various
molalities (ms, molality of potassium nitrate solutions,
0.14 0.09 0.08 0.05 0.04 0.07
molkg-1) at (288.15, 298.15, 308.15 and 318.15) K are given
in Table 1. T = 318.15 K
Standard Partial molar volumes of transfer, tV0, at Glycine 1.40 1.49 1.44 2.56 2.78 3.74
infinite dilution for some amino acids from water to 0.15
aqueous potassium nitrate solutions at 288.15, 298.15, 0. 0.15 0.16 0.19 0.22
308.15 and 318.15 K 15
DL--alanine 0.52 0.50 1.24 2.21 2.50 3.17
0 6 3 -1 -1a
tV x 10 /m mol at various mS/molkg
T=288.15 K 0.24 0.31 0.26 0.34 0.27 0.25
Amino acids 0.25 0.5 m 0.75 m 1.0 m 1.5 m 2.0 DL--amino-n-butyric 0.04 0.50 1.26 1.33 1.99 2.84
m m acid
0.24 0.25 0.25 0.26 0.22 0.23
Glycine 0.81 0.86 1.40 2.11 2.23 3.18
0.08 0.0 0.08 0.09 0.0 L-valine 0.29 0.53 1.13 1.30 1.70 2.47
9 0.09 8
0.16 0.18 0.19 0.21 0.18 0.20
DL--alani 0.31 0.43 0.64 1.40 1.72 2.22
ne 0.08 0.05 0.23 0.06 0.0 L-leucine 0.04 0.27 0.94 1.11 1.24 1.73
0.09 5
0.21 0.21 0.20 0.18 0.20 0.23
DL--amin 0.20 0.31 0.56 1.43 1.61 1.98
o-n-butyric 0.11 0.10 0.10 0.09 0.1
Apparent molar volumes of amino acids have been calculated
acid 0.10 0
as follows:
L-valine 0.13 0.17 0.29 0.79 1.12 1.33
V2,=M/(o)1000/mo(1)
0.06 0.05 0.08 0.06 0.0
Where M is the molar mass of amino acid, m (molkg-1) is the
0.06 6
molality of amino acid, and , 0 are the densities of solution
L-leucine 0.11 0.20 0.29 0.58 0.75 0.95 and solvent, respectively. At infinite dilution, the apparent
0.11 0.09 0.09 molar volumes, and partial molar volumes, are identical (V2,
0.13 0.09 0.09 0
= V2 ,). In the case of negligible concentration dependence
T = 298.15 ofV2, = V2,0was determined by taking the average of all the
K data points. However, where finite concentration dependence
Glycine 0.38 0.91 1.27 1.93 2.31 2.46 was observed,V20,was determined by least-squares fitting of
the data using the following equation:
0.10 0.04 0.03 0.02 0.04 0.11 V2,=V2,0+ Svm(2)
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International Journal of Engineering and Technical Research (IJETR)
ISSN: 2321-0869, Volume-2, Issue-2, February 2014
WhereV2,0 is the infinite dilution apparent molar volume and WhereSis the shrinkage in volume produced by the
has the same meaning as the standard partial molar volume, interactions of hydrogen bonding groups present in the solute
andSv is the experimental slope. TheV2,0values along with with water molecules and n is the potential number of
their standard deviations are summarized in Table 2 at hydrogen bonding sites in the molecule. For non-electrolytes
(288.15, 298.15, 308.15and 318.15) K. TheV2,0 values for and zwitterionic solutes the shrinkage is caused by
the amino acids increases with the increase in the electrostriction and finallyV20 can be evaluatingas:
concentration of potassiumnitrate. V20 = Vvw + Vvoid - Vshrinkage(7)
From theV2,0data, the standard partial molar volumes of WhereVshrinkageis the volume due to shrinkage caused by the
transfer, tV0, at infinite dilution from water to aqueous interaction of hydrogen bonding groups present in the solute
potassium nitrate solutions have been evaluated as with water molecules. It has been reported
follows:tV0 =V20, (in aqueous potassium nitrate) - V20,(in thatVvwandVvoidhave the same magnitude in water and in
water) (3) mixed solvents for the same class of compounds. Therefore
The tV0values for the amino acids are illustrated in Figures 1 positive tV0values can be attributed to a decrease in the
a-d
. The tV0values for the studied amino acids are positive shrinkage volume in the presence of aqueous solutions of
and increase almost linearly with the increase in concentration KNO3. Because of the stronger interactions of
of aqueous potassiumnitrate solutions. The more positive K+andNO3-withCOO-and NH3+ in the amino acids, the
tV0values in the case of glycine indicate the dominance of electrostriction of neighboring water molecules due to these
the effect of charged end groups (NH3+ and COO-),whereas charged centers/peptide backbone will be reduced which will
less positive tV0values in the case result into a reduction in the shrinkage volume.
ofDL--amino-n-butyricacid, L-valine and L-leucine indicate
the effect of the hydrophobic parts.
The cosphere model can be utilized to rationalize the
tV0values in terms of solute-cosolute interactions. According
to this model, when two solute particles come close enough
together so that their cosphere overlap some cosphere
material is displaced, and this is accompanied by the change
in thermodynamic parameters. The following types of
interactions can occur between amino acids and KNO3 in
solutions:
i. Ion-ion interactions occurring between K+
ions and COO- groups of amino acids and
between NO3-ions of potassium nitrate and
NH3+ groups of amino acids.
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Investigations of Various Amino acids in different Aqueous Solutions of Potassium Nitrate at Various Temperatures in
terms of Partial Molar Volumes
Figure 2a. Pair interaction coefficient, VXY, of some amino Figure 3c. Standard partial molar volumes of transfer, t V0 ,
acids vs. number of carbon atoms, nC, in the alkyl chain of of some amino acids vs. number of carbon atoms, nC, in the
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International Journal of Engineering and Technical Research (IJETR)
ISSN: 2321-0869, Volume-2, Issue-2, February 2014
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Investigations of Various Amino acids in different Aqueous Solutions of Potassium Nitrate at Various Temperatures in
terms of Partial Molar Volumes
temperature. This also gets support from the volumetric and 308.15 K, respectively. Therefore, as an approximation, the
compressibility studies of glycine and DL--alanine in hydration numbernH can be obtained by Eq. (9). As explained
aqueous sodium sulfate solutions by Wadi and Ramasami, earlier, addition of KNO3 decreases the electrostriction of
who reported that the hydration number of amino acids water and this also means thatnHdecreases as the
decreases with increasing temperature and concentration of electrostricted water becomes more like bulk water.
sodium sulfate. The increase in positiveV20values of studied The number of water molecules bound to the amino acids was
amino acids with the increase in the concentration of KNO3 calculated using the method reported by Milleroet al.
may further be attributed to the formation of non-covalent nH = V20 (elect) / V E0 V B0
ion-pairs between the charged groups of the amino acids and (10)
the cation (K+) and the anion (NO3-) of the electrolyte. This WhereVE0is the molar volume of electrostricted water andVB0
increases the apparent molar volume of amino acid and is the molar volume of bulk water. The electrostriction partial
decreases electrostriction of water around amino acids in the molar volume,V20(elect) can be estimated from
presence of KNO3. Further the formation of the ion-pairs also experimentally measured V20using following equation:
decreases the hydrophobicity of amino acid molecules arising V20 (elect) = V20(amino acid) V20(int) (11)
from the interactions of the hydrocarbon portion of amino The intrinsic volume,V20(int), consists of two terms: the
acids with water molecules. vander Waals volume and the void volume. V20(int) can be
The decrease in the magnitude of tV0 values with the obtained from crystal volume data. ThenH values for the
increase of temperature can be attributed to the enhanced amino acids in the presence of KNO3are less than in water and
thermal agitation and weakening of various interactions decrease with increasing concentration of KNO3, which
involving ions resulting in the relaxation to the bulk more of suggests that potassium nitrate has a dehydration effect on the
the electrostricted water molecules from the mutually amino acids. Other workers also have reported the similar
interacting regions. observations that electrolytes have a dehydration effect on
Kozak et al. have proposed formalism on the basis of amino acids. The V20,increases with increasing temperature
McMillan-Mayer theory of solutions which permits the from 288.15 to 318.15K. An increase in temperature reduces
formal separation of the effects due to interactions between the electrostriction and hence increases V20,.The reduction in
pairs of solute molecules and those due to interactions the electrostriction with increasing temperature is confirmed
involving three or more solute by the decreasednH. Therefore, temperature effect on the
molecules. Friedman and Krishnan and Franks et al. electrostriction of water by the zwitterionic centers of the
have further discussed this approach to include the amino acids is a predominant factor in determining
solute-cosolute interactions in the solvation sphere. Various temperature dependence ofV20,of the amino acids. Proposed
workers used this approach to study the interactions of amino by Hakin et al. for the infinite dilution apparent molar
acids and cosolutes in aqueous medium. The various transfer volumes of amino acids at all temperatures, these linear
functions of the amino acids can be expressed by the relations could be reasonably represented by:
following equation: V20, = V20,(NH3+, COO-) + nCV20,(CH2) (12)
tV0= 2VABms + 3 VABBms2 + 4 VABBBms3 (8) WherenC is the number of carbon atoms in the alkyl chain of
WhereVAB, VABBandVABBBare respectively, pair, triplet and the amino acids. A linear regression analysis ofV20,, values at
quartet interaction coefficients (where A stands for the amino any given temperature using equation givesV20,values at any
acids, B stands for KNO3). Using above equation volumetric given temperature using Eq. (12) givesV20,(NH3+, COO-), the
interaction parameters was calculated and are illustrated in zwitterionic end group andV20,(CH2), the methylene group
Figure 2aat 298.15K. The data reveal that all pair volumetric contributions. These results are illustrated in Figures 3a-d.
interaction parametersVABare positive for the five amino acids However, it should be pointed out that V20,(CH2) value
studied and are larger than corresponding VABB values. This obtained here characterizes the mean contribution of CH and
shows that the interactions between the amino acids and CH3 groups to V20,of the - amino acids.The alkyl chain of
KNO3 are mainly pair interactions. The pair, triplet and the homologous series of -amino acids investigated in this
quartet interactions coefficients from volumes in case of work and its contributions have been obtained using the
various -amino acids (glycine, DL--alanine, following equation proposed by Hakinet al.
DL--amino-n-butyric acid, L-valine and L-leucine) are V20,(CH3)=1.5 V20,(CH2)(13)
summarized in Table 4. The pair and quartet coefficients are V20,(CH) = 0.5 V20,(CH2) (14)
all positive while triplet negative. This shows that the pair and It can be seen that the contributions of (NH3+, COO-), groups
quartet interactions in case of two thermodynamic properties to V20,is larger than that of the CH2group and increases with
contribute positively while triplet contributions are negative. the increasing concentration of potassium nitrate which
The positive values of pair interactions occur due to the indicates that of the interactions between potassium nitrate
overlap of hydration spheres of the various -amino acids and charged end groups(NH3+, COO-) of amino acids are
(glycine, DL--alanine, DL--amino-n-butyric acid, L-valine stronger than those between potassium nitrateand CH2
and L-leucine) and KNO3 molecules, which supports the groups. TheV20,(CH2) values are almost insensitive to the
conclusion drawn earlier from the cosphere overlap model. concentration of potassium nitrate, and similar observations
V20,= V20,(int) + nH (VE0 VB0) (9) have been reported by other worker in sodium acetate.
WhereV20,(int) is the intrinsic volume of a solute However, the contribution from side chains increases with the
molecule,VE0 andVB0are the partial molar volumes of water in increasing size of side chains of amino acids. The standard
the bulk state and in the hydration shell of a solution. partial molar volumes of transfer of zwitterionic end groups
Following the procedure described by Milleroet al. 41 (VE0 [tV0(NH3+, COO-)] and alkyl side chain groups [tV0(R)]of
VB0) = -2.9, -3.3, -4.0 cm3mol-1 at 288.15 K, 298.15 K and amino acids from water to aqueous
49 www.erpublication.org
International Journal of Engineering and Technical Research (IJETR)
ISSN: 2321-0869, Volume-2, Issue-2, February 2014
potassiumnitratesolutionsare illustrated in Figures 4a-dfor equation is useful for making a distinction ionic or polar
different temperatures and have been calculated as follows: solutes and those for making a distinction between ionic or
tV0(NH3+, COO- or tV20(R) = V20(NH3+,COO-) or V20 (R)(in polar solutes and those for which hydrophobic hydration is
aqueous potassium nitrate) V20(NH3+, COO-) or V20,(R)(in dominant. The presently obtained (2V0/T2)p values are
water) (15) positive for all amino acids which suggests that studied amino
The contribution of charged end groups(NH3+,COO-)are acids are structure maker in water as well as in aqueous
positive, and those of CH2 groups are negative. From these KNO3.
observations, the overall positive tV0 values suggest that the
effect of charged end groups dominates that of alkyl side IV. CONCLUSION
chains. Partial molar volumes, V20,, of glycine, DL-amino-n-butyric
The partial specific quantities are primarily independent of acid, L-valine, L-leucine in aqueous and in mixed aqueous
the size of the solute and reflect the ratio of the effect of the
solutions of KNO3 (0.25, 0.5, 0.75, 1.0, 1.5, 2.0) molkg-1,
hydrophilic hydration on the hydrophobic hydration, whereas
have been determined at T = (288.15 to 318.15)K. From these
the partial molar quantities are the reflection of the net
data, transfer volumes, hydration numbers, and side chain
changes in both hydrations. The standard partial molar
contributions have been determined. The tV0values are
specific molar volumes,20(20= V20/M, where M is the molar
positive in all the cases, and these increase with an increase in
mass for studied amino acids) in aqueous potassium nitrate
the concentration of KNO3 and temperature. VXY values are
solutions are given in20values from glycine to L-leucine both positive, and VXYY values are negative in all cases, which
in water and in aqueous potassium nitrate solutions due to the suggest that interactions between amino acids and KNO3 are
effect of the size of the side chains of the amino acids are mainly pair wise. nH values also decrease with concentration
illustrated in Figures 5aat 298.15K. Furthermore, the value of KNO3 and temperature. These parameters suggest that
of20 increases with the concentration of potassium nitrate ion-ion interactions between charged ends of amino acids and
and a slight increase is also noted with the increase in ions of KNO3 dominate over the ion-hydrophobic interactions
temperature, again suggesting the dominance of the in these systems. The positive (2V0/T2)p values for all amino
interactions between ions of potassiumnitrate for the studied acids in aqueous KNO3suggest that studied amino acids are
amino acids tends to be linear as the size of side chains structure breakers in aqueous KNO3solutions.
increases. This may be attributed to the negative contribution
from the alkyl side chains of amino acids whose magnitude
ACKNOWLEDGMENT
increases with the size of the side chain.
The temperature dependence of V0for various amino acids in V. Dhir is very thankful to University Grants Commissions,
water and in aqueous potassium nitrate solutions, studied here India for sanctioning research project File No.8-2 (45)/ 2011
can be expressed by the general equation as follows: (MRP /NRCB)entitled Adiabatic Compressibilities of
V0=a + b T + c T2 (16). Various Amino Acids and Peptide in Aqueous Solutions of
The partial molar (limiting apparent molar) expansibilities, Various Electrolytes at Different Temperatures
E= (V/T)p, calculated from the general equation are (288.15-318.15 K).
given in Table 7. It is found that Table 7 that Evalues for
glycine, DL--alanine and DL--amino-n-butyric acid REFERENCES
increases in magnitude with increase in temperature while for [1.] I. Haq, R.R.J. Obrien, J.E. Ladbury, Drug-Receptor Thermodynamics:
Introduction and Application, Ed. R.B. Raffa. 2000, Chapter 5.
L-valine at0.25 molkg-1 (KNO3) and L-leucineat 0.25, 2.0 [2.] T.V. Chalikian, A.P. Sarvazyan, K.J. Breslauer, Biophys. Chem. 1994,
molkg-1 (KNO3) decreases with rise in temperature 51, 89.
indicating thereby that the behavior of L-valine and [3.] L.R. Murphy, N. Matubayasi, V.A. Payne, R.M. Levy, Folding Res.
L-leucineat this molalitiesare just like that of common salts, 1998, 3, 105.
[4.] J.M. Sorenson, G. Hura, A.K. Soper, A. Pertsemlidis, T. Head-Gaordon,
because in the case of common salts the molar expansibility J. Phys. Chem. B 1999,103, 5413.
should decrease with rise in temperature. It is also evident [5.] B. Sabulal, N. Kishore, J. Chem. Soc. Faraday Trans. 91,1995, 2101.
from Table 7 that the value of Eincrease in temperature for [6.] M.J. Tait, F. Franks, Nature 1971, 91, 230.
glycine, DL--alanine and DL--amino-n-butyric acid in [7.] Soto, Ana; Arce, Alberto; Khoshkbarchi, Mohammad; Vera, Jaun. Effect
of cation and anion of an electrolyte on apparent molar volume,
water. During the past few years it has been emphasized by isentropic compressibility and refreactive index of glycine in aqueous
different workers that Sv*is not the sole criterion for solutions. Biophys. Chem. 1999, 76, 73-82.
determining the structure making or structure breaking nature [8.] Wadi, R.K.; Goyal, R.K.; Temperature dependence of apparent molar
of any solute. Heplerdeveloped a technique of examining the volume and viscosity B-coefficients of amino acids in aqueous
potassium thiocyanate solutions from 15 to 35 0C, J. Solution Chem.
sign of (2V0 /T2)pfor various solutes in terms of long-range 1992, 21, 163-170.
structure making and breaking capacity of the solutes in [9.] Soto, Ana; Arce, Alberto; Khoshkbarchi, Mohammad,; Vera, Jaun. H.
aqueous solutions using the general thermodynamic Effect of cation and anion of an electrolyte on the solubility of
expression; DL--amino butyric acid in aqueous solutions: measuring and
modeling. Biophys. Chem. 1998, 73, 77-83.
(Cp / p)T =- (2V0 / T2)p(17) [10.] R.Bhat,;J.C.Ahluwalia, Partial molar heat capacities and volumes of
On the basis of this expression it has been deduced transfer of some amino acids and peptides from water to aqueous
that structure making solutes should have positive values, sodium chloride solutions at 298.15 K, J. Phys. Chem. 1985, 89,
whereas structure breaking solutes should have negative 1099-1105.
[11.] Wadi, R.K.; Goyal, R.K. Densities, viscosities, and application of
values. It has been suggested that for a structure breaking transition-state theory for water + potassium thiocyanate + amino acid
solute, the left side of the equation should be positive, and solutions at 288.15 308.15 K. J. Chem. Eng. Data. 1992, 37, 377 -
therefore (2V0/T2)pvalues should be negative for structure 386.
breaking and positive for structure making solutes. This
50 www.erpublication.org
Investigations of Various Amino acids in different Aqueous Solutions of Potassium Nitrate at Various Temperatures in
terms of Partial Molar Volumes
[12.] Basumallick, I.N.; Mohanty, R.K.; Chakraborty, U. Volumetric and [41.] M. Mizuguchi, M. Sakurai, K. Nitta, J. Solutions Chem. 26
salvation behavior of amino acids in some aqueous binaries: Part I. (1997) 579-594.
glycine, DL--alanine, and DL--aminobutyric acid in aqueous
solutions of strong electrolytes, Ind. J. Chem. A 1986, 25, 1089-1091. [42.] L. G. Hepler, Can. J. Chem. 47 (1976) 359-367.
[13.] Ogawa, T.; Yasuda, M.; Mizutani, K. The volume, adiabatic
compressibility, and viscosity of amino acids in aqueous alkali chloride
solutions, Bull. Chem. Soc. Jpn. 1984, 57 2064-2068.
[14.] Natarajan, M.; Wadi, R.K.; Gaur, H.C. Apparent molar volumes and
viscosities of some - and ,-amino acids in aqueous ammonium
chloride solutions at 298.15 K, J. Chem. Eng. Data. 1990, 35, 87-93.
[15.] S.B. Dixit, R. Bhasin, E. Rajasekaran, B. Jayaram, J. Chem. Soc.
Faraday Trans. 1997, 93, 1105.
[16.] Archer, D. G. Thermodynamic properties of the sodium chloride +water
system. Thermodynamic equilibria. J. Phys. Chem. Ref. Data1992, 21,
793829.
[17.] Hakin, A. W.; Duke, M. M.; Klassen, S. A.; McKay, R. M.; Preuss, K.
E. 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. Can. J. Chem. 1994, 72, 362368.
[18.] Kharakoz, D. P. Volumetric properties of proteins and their analogs in
diluted water solutions. Partial volumes of amino acids, at 15-55 C.
Biophys. Chem. 1989, 34, 115125.
[19.] Hakin, A. W.; Duke, M. M.; Marty, J. L.; Preuss, K. E. 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. J. Chem. Soc.,
Faraday Trans. 1994, 362368.
[20.] Duke, M. M.; Hakin, A. W.; McKay, R. M.; Preuss, K. E. 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. Can. J. Chem. 1994, 72, 14891494.
[21.] Gurney, R. W. Ionic Process in solution; McGraw Hill: New
York,1953.
[22.] Franks, F.; Qucickenden, M. A.; Reid, D. S.; Watson, B.
Calorimetricand Volumetric Studies of Dilute of Aqueous Cyclic
EtherDerivatives. Trans. Faraday Soc. 1970, 66, 582-589.
[23.] F. Shahidi, P G Farrell, J.T. Edwards,J. Solution chem. 1976, 5,
807.
[24.] S. Terasawa, H. Ituski, S. Arakawa, J. Phys. Chem. 1975, 79,
2345.
[25.] A. Bondi, J. Phys. Chem. 1964, 68, 441.
[26.] A. Bondi, in Physical Properties of Molecular Crystals, Liquids
and Glasses, John Wiley, New York, 1968, Ch. 14.
[27.] A. Bondi, J. Phys. Chem. 1954, 58, 929.
[28.] R. K. Wadi and P.K. Ramasami, J. Chem. Soc. Faraday
Trans.1997, 93, 243.
[29.] A. Soto, A. Arce, K.M. Khoshkbarchi, Biophys. Chem. 1999, 76,
73.
[30.] J.J. Kozak, W. Knight, W. Kauzmann, J. Chem. Phys. 1968, 68,
675.
[31.] W.G. McMillan, J. Mayer, J. Chem. Phys., 1945, 13, 276.
[32.] H.L. Friedman, C.V. Krishnan, in Water-A Comprehensive
Treatise, Plenum Press, New York, 1973, Vol. 3, Ch. 1.
[33.] F. Franks, M. Pedley, D.S. Reid, J. Chem. Soc. Faraday Trans.1.
1976, 72, 359.
[34.] A. K. Mishra, J.C. Ahluwalia, J. Chem. Soc. Faraday
Trans.1.1981, 77, 1469.
[35.] Millero, F. J.; Antonio, L. S.; Charles, S. The apparent molar
volumesand adiabatic compressibilities of aqueous amino acids at 25
C. J. Phys. Chem. 1978, 82, 784792.
[36.] J. Wang, Z. Yan, K. Zhuo, D. Liu, Z. Phys. Chem. 214 (2000)
333-345.
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