MCDB 110 - Midterm I KEY - 2024

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School

University of California, Santa Barbara *

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Course

110

Subject

Biology

Date

May 18, 2024

Type

pdf

Pages

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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