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ACS Biochemistry Exam Questions And Answers (Guaranteed A+)

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©FYNDLAY EXAM SOLUTIONS 2024/2025 ALL RIGHTS RESERVED. 1 | P a g e ACS Biochemistry Exam Questions And Answers (Guaranteed A+) Describe the structural changes in hemoglobin that allow for cooperative binding of O2 - answerBinding 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? - answerAsp, Glu, Arg, His, Lys Which amino acids are negatively charged? - answerAsp, Glu which amino acids are positively charged? - answerArg, His, Lys How are beta sheets stabilized in proteins? - answerHydrogen bonding between peptide backbone groups Does myoglobin show cooperativity in O2 binding? If not, what structural differences account for this? - answerMyoglobin 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? - answerSimilar 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

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©FYNDLAY EXAM SOLUTIONS 2024/2025

ALL RIGHTS RESERVED.




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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