ACS Biochemistry Exam Questions And
Answers (Guaranteed A+)
Describe the structural changes in hemoglobin that allow for cooperative binding of O2 -
answer✔Binding of O2 in one subunit causes a conformational change in an adjacent subunit
allowing O2 to bind
Which amino acids in "a" would be charged at pH 7? - answer✔Asp, Glu, Arg, His, Lys
Which amino acids are negatively charged? - answer✔Asp, Glu
which amino acids are positively charged? - answer✔Arg, His, Lys
How are beta sheets stabilized in proteins? - answer✔Hydrogen bonding between peptide
backbone groups
Does myoglobin show cooperativity in O2 binding? If not, what structural differences account
for this? - answer✔Myoglobin does not show cooperativity because it is monomeric
What is a transition state inhibitor (how does its structure compare to the enzyme stubstrate?)
how does its affinity for the enzyme compare to the enzyme's substrate? - answer✔Similar to
the substrate; binds to the active site with greater affinity than the substrate
would it be advantageous for these potential drugs to covalently bind to the enzyme? why or
why not? - answer✔Not advantageous because the urea cycle would shut down
From a practical standpoint, would it be advantageous for these potential drugs to be less
chemically stable than the substrate? - answer✔No, because of shelf life and time to reach
target
In DNA, which bases hydrogen bond? - answer✔A-T; G-C
In each base pair, how many hydrogen bonds are there? - answer✔A-T=2; G-C=3
Which base-pair would require a higher temperature to destroy the hydrogen bonds? -
answer✔G-C
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