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* Aided by a grant from The Chemical Foundation, Inc., and the Re-
starch Board of the University of California.
We are indebted to the Cyrus M. Warren Fund of the American Academy
of Arts and Sciences for the loan of the galvanometer used in these
experiments.
161
162 Thermodynamic Data of Amino Acids
The van? Hoff equation is strictly true only when Henry’s law is
obeyed; that is, when the mole fraction and the activity are pro-
portional. In dilute solutions where the molality is proportional
(4, 15, 16). Several properties of the amino acids suggest that
they exist in solution in the form of zwittcr ions (17, 18). How-
ever, Scatchard and Kirkwood (19), from theoretical considera-
tions, have calculated that the thermodynamic properties of
zwitter ions will be directly proportional to their concentration.
In this respect they would behave like non-electrolytes. It was
considered of interest to determine whether solutions of amino
acids would show heat capacities and heat contents similar to
solutions of electrolytes or non-electrolytes.
Technique
The amino acids used were crystallized several times from water
2 In the case of lysine this was not met, as the total nitrogen was 1.2 per
cent low. Contamination with a small amount of barium sulfate, produced
during the isolation, probably caused the deviation found. Owing to the
difficulty of crystallizing this very soluble amino acid, no further purifica-
tion was attempted. The error produced in the heat effect measured is
probably within the limits of error of the temperature measurement.
C. A. Zittle and C. L. A. Schmidt 165
TABLE I
Specijic Heat and Heat Capacity of Aqueous Solutions of Glycine, d&Alan&e,
cP,
capmity
% CP,
I I Spe-
oifio
Heat capacity
I 6 I %- I-
Heat capacity
ZP,
-- --- --
cd./ Cal./
M cd. cd. cd. (de%)- cd cd. cd.
22i
0 0.998 7.5 7.5 17.9t I.998 40 40.0 17.980.993 93 93 17.96
0.2 0.9% 8.5 7.5 17.9f I.988 39 39.5 17.980.993 84 90 18.01
0.5 0.961 9.0 8.0 17.9; I.974 37 38.0 17.990.983 69 85 18.09
0.63 0.976 63 82 18.15
1.0 0.93f 11.5 8.5 17.91 I.950 34 37.0 18.04
1.5 0.91( 14.0 9.5 17.9( I.928 31 35.5 18.13
1.88 1.910 29 35.0 18.16
2.0 0.8% j 16.5 11.0 17.&
2.5 0.86; r 19.5 13.0 17.7:
3.0 0.851 I 22.0 15.0 17.6(
3.33 0.84 ) 23.5 15.5 17.5(
- , I
-
TABLE II
Heats of Solution, in Calories per Mole, and Temperature Coejkients of
Certain Amino Acids from Solubility Measurements at !Z5’*
- -
* The uncertainty is indicated for the most concentrated solution measured. In more dilute solutions, where the heat
effects are smaller, the percentage uncertainty is greater.
tegration in the very dilute region. The data obtained for the
integral heats of dilution are given in Table III as $0h- cp”h (only
those for the saturated solutions were measured; the others were
calculated). The values calculated for 82 - ROz are given in
Table III.
In Table IV the integral heat of dilution of glycine calculated
from the heat content of the constituents is given, together with
those obtained by direct measurement. The values for the two
most concentrated solutions were obtained in this study. Those
for the more dilute solutions were reported by Naude (4) from
measurements at 18”. A calculation of the change of the heat of
dilution with change in temperature gave a decrease of 0.5 calorie
per degree of rise in temperature for the 1 M solution. This would
C. A. Zittle and C. L. A. Schmidt 171
make Naude’s value for this concentration 121 calories at 25”.
In the more dilute solutions the change is less. It is characteris-
tic of non-electrolytes that changes in heat content accompanying
dilution are zero or very small in concentrations even as large as
0.1 M. This is correlated with their forming perfect solutions at
these concentrations. In the case of electrolytes the heat of dilu-
tion of a 0.01 M monovalent salt is about -42 calories per mole
(16, 4).
The relative partial molal heat contents of solvent and solute
can also be obtained by transferring measured quantities of solu-
tion of known molality into such a quantity of pure water that an
infinitely dilute solution is formed. In this case the heat contents
can be calculated without the difficulties of integration found for
the procedure in which water is transferred into the solution. The
TABLE VI
Heat of Solution, in Calories per Mole, of Certain Amino Acids at 25”
0 i F.2(r&u-
Amino acid j v,” - H,(solid) p ,“- (D,, (saturated)* 2 -fqsat. .) Ixted) -
1‘Iz (solid)
- -_
Glycine. 3755 f 15 225 400 3355
values given above for 0” are too low, the third too high. The
value of 0.90 for the saturated solution at 25” will be used in the
free energy calculations. A similar calculation made for dl-
alanine with (a, - 802) as a function of temperature gave a 6
per cent decreasein the activity for the sametemperature change.
Calculations for dl-valine, with (If2 - I?.J as a constant, gave a
decreaseof 5 per cent.
The free energy change for the reversible transfer of a mole of
solid glycine into a 3.33 M aqueous solution was calculated by the
use of Equation 3. At 25” the value for AF is zero for the above
process, since the solution is saturated. The change in heat con-
tent for this transfer is 3350 calories and dAH/dT is -9 calories.
Similar calculations were made for I-aspartic acid with the fol-
lowing data: AH solution, 5790 calories; dAH/dT, 41 calories; ( a2
- 80~)~ -400 calories; AF, per mole, for the transfer of the un-
ionizedmolecule froma 1 M (standard solution) to a 0.038 M solution
where the percentage ionized is 93.5 and yU273is 0.42, -2450
calories. The following equations were obtained.
AF (solid ti 0.038 M) = -94.4OT log T - 6410 + 254.31 (15)
AF(l M ti 0.038 M) = -9.572’ + 400 WV
182 Thermodynamic Data of Amino Acids
At 298” AF (solid @ 1 M) is 2450 calories; at 310’ the change in
free energy for the same transfer is 2150 calories. Borsook and
Huffman (13) have obtained 2160 and 1940 calories respectively
for this transfer by the use of solubility data at the higher tem-
perature and an activity coefficient calculated by the use of the
dissociation constant. The difference is due chiefly to the values
of yU used. The value of yu and the percentage of un-ionized as-
partic acid used above were taken from the data of Hoskins,
Randall, and Schmidt (7). (R, - 802) was estimated from the
behavior of dl-glutamic acid and is only approximate; it was con-
sidered as being entirely caused by the change in the activity of
the un-ionized molecule.
SUMMARY
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