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acid
proton donor
base
proton acceptor
Ionization of H20
H2O + H2O → H3O+ + OH-
A + B → CA + CB
equilibrium water constant
kw = 10-14
[H+] > 10-7
acid
[H+] < 10-7
base
pH =
-log[H+]
Henderson-Hasselback Equation
pH = pka + log [A-]/[HA]
if low pKa
will be deprotonated above its pKa
if high pKa
will be deprotonated below its pKa
amine groups
never have a negative charge
if more base than acid [A-] > [HA+]
species will be deprotonated at neutral
if more acid than base [A-] < [HA+]
species will be protonated at neutral
Kw =
Keq * [H2O]
-log[H+] - log [OH-] =
+14
ka increases
if concentration of acid increases
if pH > pKa
base > acid
deprotonation
if pH < pka
acid > base
so protonation!
pH
acidity of the environment
pKa
point of deprotonation and protonation
buffer range
pKa +- 1
in proteins, COOH is deprotonated more at higher pH values
so the more basic the solution, the more negative the charge of the protein
the more acidic the solution, the more positive the charge of the protein
what is a buffer
weak acids + salts
weak base + salts
resist change +- 1
at +-2 the group is either fully protonated/deprotonated
pH = pKa
50% deprotonated and 50% ionized
pI (isoelectric point)
pH where the average charge on the molecule is zero
average of the two pKa values surrounding the isoelectric species
pI = pKa + pKb/2
pKa of H3N+
9.6
pKa of COO-
2.3
increase the pH of an amino acid
more negatively charged the amino acid will be
decrease the pH of an amino acid
more positively charged the amino acid will be
strong acids disassociate fully
weak acids don’t
determining pH of a weak acid
ka= [H+][A-]/[HA]
when to ignore x in weak acid disaasociation
x ➗initial conc is <5%
c ➗ ka > 100
eliminate x when k <= to a number x 10-4