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3.0
2.5
2.0
1.5
0.0
0.5
1.0
1.5
2.0
2.5
3.0
10.0
9.0
8.0
7.0
0.0
0.5
1.0
1.5
2.0
2.5
3.0
12.0
11.0
10.0
9.0
0.0
0.5
1.0
1.5
2.0
2.5
3.0
I
0.5
Figure 2.2.
Values of dissociation constants of cysteine in NaCl solution at different
temperatures (
, 5°C;
, 25°C;
, 45°C; solid lines are a second-order fit of the
p
K
i
*
vs. I
0.5
) (adapted from Sharma et al. [40] with the permission of Springer America).
proteins for alkali cations can evaluate competition from trace metals (e.g., Fe,
Cd, Zn, and Co) to bind Cys at protein sites.
Studies on the effect of polarity of organic solvents on the p
K
i
of amino
acids have been performed [3, 70]. Understanding of solvent effect is essential
considering the influence of polarity on stabilization/destabilization on protein
structure. Polarity of water is expected to be lower at the active sites of pro-
teins in the biological systems. Dissociation of amino acids has therefore been
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