BIOC 384 - SW 6 2024/2025 Exam
Questions with Detailed Verified
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Which of the following amino acids is most likely to be found lining the
hydrophobic substrate channel of an enzyme? - 🧠ANSWER
✔✔phenylalanine
Which of the following would you expect to be excluded from entering this
hydrophobic substrate channel? - 🧠ANSWER ✔✔H2O and Ca2+
The maximum velocity - 🧠ANSWER ✔✔A. is the velocity where addition of
more substrate does not cause a velocity increase.
Label the parts of the Michaelis-Menten graph. (Note: The pink line
represents the enzyme reaction with a high concentration of enzyme, while
the green line represents the same enzyme reaction with a lower enzyme
concentration.) - 🧠ANSWER ✔✔From Top to Bottom on chart:
B(Vmax) --> C (1/2 Vmax) --> A (Km)
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, The active site of chymotrypsin is made up of - 🧠ANSWER ✔✔Asp102 and
His57 from the B chain and Ser195 from the C chain.
Which of the following biochemical concepts does the animation best
illustrate? - 🧠ANSWER ✔✔The three-dimensional final folded structure of
enzymes is critical for the formation of catalytic sites that may not be
predicted solely by primary sequence alone.
Label the following figure. (Not all labels may be used.) Remember that an
enzyme's active site binds to substrate based on the shape of both the
enzyme and active site, as well as the attraction between amino acid
residues (or cofactors) in the active site and on the substrate. For example,
opposite charges will attract one another, and nonpolar residues will attract
one another. - 🧠ANSWER ✔✔- A (Hydrophobic regions) and D (Charged
residues) ON TOP HALF
- B (Enzyme-substrate complex with induced-fit binding to substrate) ON
BOTTOM HALF
Enzyme (E) affinity for substrate (S) can be estimated by determining how
much substrate [S] is required to fill half of available binding sites. Use the
information in the table above to assess the relative affinities of each
enzyme, and rank order the enzymes from Highest Affinity (on the left) to
COPYRIGHT©JOSHCLAY 2025/2026. YEAR PUBLISHED 2025. COMPANY REGISTRATION NUMBER: 619652435. TERMS OF USE. PRIVACY
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STATEMENT. ALL RIGHTS RESERVED
Questions with Detailed Verified
Answers (100% Correct Answers) |
Already Graded A+
Which of the following amino acids is most likely to be found lining the
hydrophobic substrate channel of an enzyme? - 🧠ANSWER
✔✔phenylalanine
Which of the following would you expect to be excluded from entering this
hydrophobic substrate channel? - 🧠ANSWER ✔✔H2O and Ca2+
The maximum velocity - 🧠ANSWER ✔✔A. is the velocity where addition of
more substrate does not cause a velocity increase.
Label the parts of the Michaelis-Menten graph. (Note: The pink line
represents the enzyme reaction with a high concentration of enzyme, while
the green line represents the same enzyme reaction with a lower enzyme
concentration.) - 🧠ANSWER ✔✔From Top to Bottom on chart:
B(Vmax) --> C (1/2 Vmax) --> A (Km)
COPYRIGHT©JOSHCLAY 2025/2026. YEAR PUBLISHED 2025. COMPANY REGISTRATION NUMBER: 619652435. TERMS OF USE. PRIVACY
1
STATEMENT. ALL RIGHTS RESERVED
, The active site of chymotrypsin is made up of - 🧠ANSWER ✔✔Asp102 and
His57 from the B chain and Ser195 from the C chain.
Which of the following biochemical concepts does the animation best
illustrate? - 🧠ANSWER ✔✔The three-dimensional final folded structure of
enzymes is critical for the formation of catalytic sites that may not be
predicted solely by primary sequence alone.
Label the following figure. (Not all labels may be used.) Remember that an
enzyme's active site binds to substrate based on the shape of both the
enzyme and active site, as well as the attraction between amino acid
residues (or cofactors) in the active site and on the substrate. For example,
opposite charges will attract one another, and nonpolar residues will attract
one another. - 🧠ANSWER ✔✔- A (Hydrophobic regions) and D (Charged
residues) ON TOP HALF
- B (Enzyme-substrate complex with induced-fit binding to substrate) ON
BOTTOM HALF
Enzyme (E) affinity for substrate (S) can be estimated by determining how
much substrate [S] is required to fill half of available binding sites. Use the
information in the table above to assess the relative affinities of each
enzyme, and rank order the enzymes from Highest Affinity (on the left) to
COPYRIGHT©JOSHCLAY 2025/2026. YEAR PUBLISHED 2025. COMPANY REGISTRATION NUMBER: 619652435. TERMS OF USE. PRIVACY
2
STATEMENT. ALL RIGHTS RESERVED
