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CHEM 210 Module 3 Exam Newest Questions and Answers 2025 (Verified Answers), Exams of Chemistry

CHEM 210 Module 3 Exam Newest Questions and Answers 2025 (Verified Answers) True or False: The amino acids serine and threonine both contain sulfur atoms.

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2024/2025

Available from 06/16/2025

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CHEM 210 Module 3 Exam Newest Questions and Answers
2025 (Verified Answers)
Question 1
3 / 3 pts
True or False: The amino acids serine and threonine both contain sulfur atoms.
FALSE
True or False: The following secondary structure shown below is an example of a
beta- turn.
FALSE
True or False. The side chain of phenylalanine is bonded to the backbone
nitrogen atom.
FALSE
True or False: The name of the molecule that binds to an enzyme is called the
holoenzyme.
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Question 2

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Question 3

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CHEM 210 Module 3 Exam Newest Questions and Answers

2025 (Verified Answers)

Question 1

3 / 3 pts True or False: The amino acids serine and threonine both contain sulfur atoms. FALSE True or False: The following secondary structure shown below is an example of a beta- turn. FALSE True or False. The side chain of phenylalanine is bonded to the backbone nitrogen atom. FALSE True or False: The name of the molecule that binds to an enzyme is called the holoenzyme.

Question 5

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FALSE

Question 8

3 / 3 pts The peptide Ala-Glu-Gly-Ala-Leu has.

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Question 9

3 / 3 pts A disulfide bond Five peptide bonds Four peptide bonds A proline residue No C-terminal FOUR PEPTIDE BOND Formally, when there are 100 or more amino acids are covalently linked together that is called a. Polypeptide Oligopeptide Peptide Protein Polyprotein PROTEIN What unit is used by biochemists to indicate the mass of a protein? kDa kBa Mol/g g/mol kg kDa

Question 13

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Question 12

3 / 3 pts A) α carbon B) Carboxyl group C) Amino group D) carbon E) None of the above A) a carbon Which of the following correctly matches the amino acid with its one letter abbreviation? Glutamic acid, E Isoleucine, S Lysine, L Phenylalanine, P Arginine, A GLUTAMIC ACID, E The order of amino acids in a protein is written. 3’ to 5’ 5’ to 3’ N to C- terminus C to

N-terminus Smallest to largest amino acid by weight N TO C-TERMINUS

Question 14

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CONTENT AND ARRANGEMENT OF THE SECONDARY STRUCTURE

The secondary structure shown below is an example of a(n):

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Question 18

3 / 3 pts Parallel beta sheet Antiparallel beta sheet alpha helix beta-turn alpha- turn ANTIPARALLEL BETA SHEET The overall three-dimensional shape of a single folded polypeptide is structure. Primary Secondary Tertiary Quaternary Motif TERTIARY

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Question 20 3 / 3 pts An enzyme requires Cr+3 for catalysis. When the enzyme contains the Cr3+ it called a/an. Holoenzym e Apoenzyme Fully ready molecule Inhibitor Competitive inhibitor HOLOENZYME

As a substrate reacts to become a product, it goes through the , which is a high potential energy state. Conversion State Stable mode Unstable mode

Enzyme- specificity Enzyme- substrate Energy-specificity Energy- substance Both B and D

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Question 25

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ENZYME-SUBSTRATE

Any molecule or ion that is necessary for an enzyme’s function is called a: Cofactor Coreactant Coproduct Bienzyme Both B and C COFACTOR Consider the following protein structure. A) Is the protein globular or fibrous? Explain your response in at least one complete sentence giving at least one (1) piece of evidence in your response. B) Identify at least two (2) types of secondary structure present in the following protein. A) Globular proteins are ball-like in shape, while fibrous proteins are extended. Note the long strands of alpha-helices. B) Point out the two types of secondary structure shown here in this protein (as indicated in

(short response) Hemoglobin is said to be a tetramer. A) What is a tetramer? B) Structurally, a tetramer describes what level of protein organization? Your Answer: A. A tetramer is a protein that has four subunits. Two of the subunits are called alpha subunits while the other two are called beta subunits. B. A tetramer describes the quaternary structure A) Simply it means that hemoglobin has four subunits or four independent polypeptide chains interacting non-covalently. Each protein molecule is composed of two copies each of two different subunits a and b. We say that hemoglobin is a tetramer because it has four polypeptide chains. B) It is describing the quaternary structure, which has two or more independent polypeptide chains that associate with one another to form a quaternary structure.

Question 28

5 / 5 pts (short response) There are collections of protein structure that fit between true secondary and true tertiary structure. What is the name of the collections of protein structure? Explain this type of structure. Motifs occupy a position between secondary and tertiary. Motifs are particularly stable arrangements of secondary structure, including the connections between them. Motifs are found in a variety of proteins from across all organisms.

Question 29

5 / 5 pts (Short response) A. Define the primary level of protein structure. B) How do scientists communicate the primary sequence? The primary level is the order of amino acids covalently bonded together, including disulfide bonds, in a polypeptide chain. The primary sequence is written, for proteins, from N to C terminal using the one-letter or three- letter abbreviations.

Question 30

5 / 5 pts Define the term “active site.” Your Answer: