What does pH represent in relation to hydrogen ions?
pH is the negative logarithm of the hydrogen ion concentration, expressed as pH = -
log{H+}.
What is the significance of pKa in relation to ionization?
pKa is the pH at which a molecule is 50% ionized, indicating the strength of an acid.
How does the dielectric constant affect pKa modulation?
A lower dielectric constant increases electrostatic attraction, making it easier for
charges to 'see each other' and thus increasing pKa.
What role do hydrogen bonds play in pKa modulation?
Hydrogen bonds can increase the pKa of acidic groups.
How does temperature influence the pH of buffers?
The pH of some buffers decreases as temperature increases.
What is the effect of a hydrophobic environment on acidic side chains?
In a hydrophobic environment, acidic side chains prefer to be uncharged, raising their
pKa.
What is the mechanism of aspartyl proteases?
Aspartyl proteases use an acid-base mechanism involving two conserved aspartic acid
residues in their active site to break peptide bonds. The pKa of the active site is 3.8, so
most aspartyl proteases work best at low pHs
hydrophobic amino acids
alanine, valine, isoleucine, leucine, methionine, phenylalanine, tyrosine, tryptophan,
cysteine, glycine
hydrophilic amino acids
lysine, arginine, histidine, aspartate, glutamate, serine, threonine, asparginine,
glutamine
hydrophilic basic amino acids
lysine, arginine, histidine
hydrophilic acidic amino acids
aspartate, glutamate
, hydrophilic amino acids with uncharged r groups
serine, threonine, asparginine, glutamine
amphipathic amino acids
proline
alanine
ala, a
hydrophobic
Valine
val, v
hydrophobic
isoleucine
ile, i
hydrophobic
leucine
leu, l
hydrophobic
methionine
met, m
hydrophobic
phenylalanine
Phe, F
hydrophobic
Tyrosine
tyr, y
hydrophobic
tryptophan
trp, w
hydrophobic
cysteine
cys, c
hydrophobic
can form disulfide bonds between two cysteines to stabilize extracellular proteins
glycine
gly, g
hydrophobic