Book Notes- Biochem Flashcards
L amino acids have the amino group on the _____ hand side
on the Left hand side
All chiral amino acids used in eukaryotes are ____ amino acids
“L” amino acids
amphoteric species
can either accept or donate a proton
at low pH, ionizable groups tend to be (protonated or deprotonated)
At low pH, ionizable groups tend to be protonated
All amino acids have at least ___ pkA value(s) and name the pKa value
they have two pKa values, with pKa1 around 2 and pKa2 around 9-10; amino acids with ionizable side chains have three pKa values.
At very acidic pH values, amino acids tend to be ____charged
positively charged for acidic pH values
How to calculate the pI for an acidic amino acid
pI = (pKa,Rgroup+pka,COOHgroup)/2
How to calculate the pI for a basic amino acid
pI = (pka,NH3+group + pKa,Rgroup)/2
Peptide bond formation
condensation or dehydration reaction and acyl substitution reaction–the electrophicic carbonyl carbon of the first amino acid is attacked by the nu amino group on the 2nd amino acid, then the hydroxyl group of the COOH is kicked off and the resulting formaiton is a peptide (amide) bond
primary strucutre
linear arragnement; sequence of amino acids
secondary structure
reuslt of H bonding; alpha helices and β-pleated sheets
what kinds of groups are found on the amamino acid surface of proteins?
hydrophilic (polar)
What happens when you put hydrophobic side chains in aqueous solution?
(what happens to entropy, favorable or unfavorable, and spontaneous or nonsponateous?)
entropy decreases, unfavorable, nonspontaneous
two main causes of denaturation
heat and solutes
Inhibitor that produces parallel lines
Uncompetitive
Relationship between Km and affinity
Inverse
In mixed inhibition, if it prefers the enzyme, Km…
Km increases when it prefers the enzyme
In mixed inhibition, if it prefers the substrate complex, Km…
decreases
Vmax changes in everything EXCEPT
competitive inhibitors
Hill coefficient
if > 1 = cooperative binding
