MCDB 110 - Midterm I KEY - 2024
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Course
110
Subject
Biology
Date
May 18, 2024
Type
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16
Uploaded by ProfessorCapybaraPerson1715
Howdy 110ers,
Just a breakdown of the grades and explanation of moving forward.
Complete the
Exam Wrapper
(due May 16th, 11:59PM) by correcting your exam and
submitting on Canvas. Even if you earned perfect grades, complete the reflection on
your approach. Below I include descriptive statistics to orient yourself on how the class
is doing holistically; however, this course is
NOT curved
- so the only person you are
competing against is yourself!
If you would like to chat about strategies to improve for midterm II, complete the exam
wrapper and swing on by office hours. Remember, this is just a grade on your approach
to MCDB 110 - not an evaluation of your merits as a student.
Regrades: you have 1 week to request this, but the TA will regrade your
entire
exam.
They have been generous with the grading breakdown, so ensure that your request is
based on the rubric as posted below.
Average ~ 82/100
Name______________________ Discussion section: ________________
Perm #_______________________
MCD Biology 110
Midterm I
Spring 2024
PLEASE PRINT YOUR NAME ABOVE. BE SURE THIS PACKET
CONTAINS ALL 12 PAGES.
CALCULATORS ARE ALLOWED.
READ THESE INSTRUCTIONS:
For questions number 1-30 enter your answers on the Scantron form by
filling in the appropriate bubble(s) with a #2 pencil. For the remaining
questions, write your answer to each question clearly on this exam packet.
For the problems involving calculations, your work must be shown in the
space provided to receive any credit.
Note: charges are not shown
True or False (22 points)
. Indicate the appropriate answer.
Enter A = True; B = False on the Scantron form
.
1. An amino acid is typically around 100 nm in size.
F
2. The net dipole on H
2
O confers polarity to the molecule.
T
3. Protein beta sheets are stabilized by H-bonds between amino acid R groups.
F
4. Amino acids L and V are homologues.
T
5. Strong acids are poor biological buffers as they have small Ka, indicating full
dissociation.
F
6. By lowering the activation energy, enzymes speed up reactions in both the forward
and reverse directions.
T
7. Phosphorylation is a common strategy for reversible regulation of enzyme function.
T
8. K
m
= ½ V
max
F
9. Oleic acid (C18:1
Δ9
) has a lower melting point than linoleic acid (C18:2
Δ9,12
).
F
10. Scents, hormones, water barriers are all functions served by lipid molecules.
T
11.Triglycerides, phospholipids, and waxes all include esterified fatty acids.
T
Matching: (16 points).
For each word or phrase in column one, provide the single
response from column II that
best
matches it. Enter the correct letter or letters by filling
in the appropriate bubbles on the Scantron. For example, if the best match is ab, then
fill in the bubbles for both a) and b) on the Scantron. (For this example, no credit would
be given if only one bubble is filled in). An answer from the right may be used only once.
Column I
Column II
12. __ zymogen/proenzyme
a. Strong, covalent force
13. __ Phosphoric acid (H
3
PO
4
)
b. Binds to active site
14. __ competitive inhibitor
c. ensures a reaction is reversible
15. __ D and L forms of lysine
d. determines whether a reaction is exergonic
16. __ triglycerides
e. Small pKa
17. __ ΔG
‡
ab. Electrostatic interaction
18. __ Van der Waal’s
ac. proportional to enzyme concentration
19. __ Vmax
ad. diastereomers
ae. contains three fatty acids
bc. blood buffer
bd. basic R group
be. detergent-like activity
cd. chymotrypsinogen
ce. parameter that determines rate of reaction
de. hormone signaling
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