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ACS biochemistry Guide Questions with Solutions
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ACS biochemistry Guide
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ACS biochemistry GuideDescribe 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
substrate?) 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? - answerNot 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? - answerNo, because of shelf life and time to
reach target
In DNA, which bases hydrogen bond? - answerA-T; G-C
In each base pair, how many hydrogen bonds are there? - answerA-T=2; G-C=3
Which base-pair would require a higher temperature to destroy the hydrogen bonds? -
answerG-C
Based on the mechanism of alkaline hydrolysis of RNA, why is DNA less susceptible to
alkaline hydrolysis? - answerDNA lacks the 2' hydroxyl group
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