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Chem 210 Module 3 Exam, Exams of Biochemistry

Portage Learning Chemistry 210 Module 3 Exam

Typology: Exams

2022/2023

Available from 08/21/2023

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Module 3 Exam - Requires Respondus LockDown
Browser + Webcam
Due No due date Points 100 Questions 30 Time Limit 120 Minutes
Requires Respondus LockDown Browser
Attempt History
Attempt Time Score
LATEST Attempt 1 30 minutes 90 out of 100
Score for this quiz: 90 out of 100
Submitted Apr 4 at 3:09pm
This attempt took 30 minutes.
0 / 3 pts
Question 1
True or False: The amino acids cysteine and methionine both contain
sulfur atoms.
True
orrect Answer
orrect Answer
False
ou Answered
ou Answered
3 / 3 pts
Question 2
True or False: The following secondary structure shown below is an
example of an Antiparallel beta sheet.
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pf4
pf5
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pf9
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Partial preview of the text

Download Chem 210 Module 3 Exam and more Exams Biochemistry in PDF only on Docsity!

Module 3 Exam - Requires Respondus LockDown

Browser + Webcam

Due No due date Points 100 Questions 30 Time Limit 120 Minutes

Requires Respondus LockDown Browser

Attempt History

Attempt Time Score

LATEST Attempt 1 30 minutes 90 out of 100

Score for this quiz: 90 out of 100

Submitted Apr 4 at 3:09pm

This attempt took 30 minutes.

Question 1^0 / 3^ pts

True or False: The amino acids cysteine and methionine both contain

sulfur atoms.

orrect Answerorrect Answer True ou Answeredou Answered False

Question 2^3 / 3^ pts

True or False: The following secondary structure shown below is an

example of an Antiparallel beta sheet.

True Correct!Correct! False

Question 3^3 / 3^ pts

True or False. The side chain of histidine is bonded to the backbone

nitrogen atom.

True Correct!Correct! False

Question 4^3 / 3^ pts

True or False: The name of the molecule that binds to an enzyme is

called the holoenzyme.

True Correct!Correct! False

Question 5^3 / 3^ pts

Isomerization Double-bond breaking

Question 8^3 / 3^ pts

The peptide Ala-Glu-Gly-Ala-Leu-Arg has ______.

A disulfide bond Correct!Correct! Five peptide bonds Four peptide bonds A proline residue No C-terminal

Question 9^0 / 3^ pts

Formally, when there are 99 or fewer amino acids are covalently linked

together that is called a _________.

orrect Answerorrect Answer Polypeptide

Oligopeptide Peptide ou Answeredou Answered Protein Polyprotein

Question 10^3 / 3^ pts

What unit is used by biochemists to indicate the mass of a protein?

g/mol Correct!Correct! Da

Ba Mol/g g

Question 11^3 / 3^ pts

All of the 20 standard amino acids contain an R-group that is attached to

the:

A) carbon

B) Carboxyl group

C) Amino group

D) carbon

E) None of the above

Correct!Correct! A

B C

Question 14^3 / 3^ pts

In one turn of a helix, there approximate _________ amino acids.

Correct!Correct! 3.

None of the above

Question 15^3 / 3^ pts

In an alpha helix, the R groups on the amino acid residues:

Alternate between the inside and outside of the helix Cause only left-handed helices to form Generate the hydrogen bonds that form the helix Stack within the interior of the helix Correct!Correct! Are found on the outside of the helix spiral

Question 16^3 / 3^ pts

Motifs are classified primarily by their:

Amino acid sequence Evolutionary relationships Correct!Correct! Content and arrangement of the secondary structure Content and arrangement of the tertiary structure Subunit content and arrangement

Question 17^0 / 3^ pts

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

orrect Answerorrect Answer Parallel beta sheet

Antiparallel beta sheet alpha helix

Question 20^3 / 3^ pts

An enzyme requires Cr for catalysis. When the enzyme contains the

Cr it called a/an _________.

3+

Correct!Correct! Holoenzyme

Apoenzyme Fully ready molecule Inhibitor Competitive inhibitor

Question 21^3 / 3^ pts

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 Conversion Mode Correct!Correct! Transition state

Question 22^3 / 3^ pts

What three factors influence the rate of an enzyme-catalyzed reaction?

pH, polarity, and concentration pH, polarity, and temperature polarity, concentration, and temperature amino acids, concentration, and temperature Correct!Correct! pH, concentration, and temperature

Question 23^3 / 3^ pts

The concept of induced fit refers to the fact that:

When a substrate binds to an enzyme, the enzyme induces loss of water Enzyme specificity is induced in the enzyme-substrate The enzyme-substrate binding increases the temperature Correct!Correct! Substrate binding induces a conformation change in the enzyme

The substrate bends and twists before it binds to the enzyme

Question 24^3 / 3^ pts

The ES stands for:

Your Answer:

This protein pictured above is globular (more "ball like"). The types of

secondary structures present are alpha helices, the coiled structures,and

beta sheets, the repetitive parallel sheet-like structures.

A) It is a globular protein because of its ball-like shape.

Fibrous proteins are usually long and extended. B) There is

one alpha helix in front and some in the back. Also present is

a beta sheet; there seems to be both parallel and antiparallel

strands here. Beta turns may be present, but are not required

in the answer.

Question 27^5 / 5^ pts

Your Answer:

(short response) Hemoglobin is said to be a tetramer. A) What is a

tetramer? B) Structurally, a tetramer describes what level of protein

organization?

Hemoglobin is a tetramer, a protein with four subunits. Two subunits are

called alpha subunits, and the other two are beta subunits. The structural

level of protein organization a tetramer describes is called quaternary

structure, which contains more than two independant subunit structures.

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

Your Answer:

(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.

The collections of protein structure that fit between the true secondary

and true tertiary structures are motifs. These arrangements are stable and

occupy arrangements of secondary structures. This structure is found in

many different proteins.

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.

The active site is the spot on the enzyme where catalysis

takes place. This area is often small when compared to the

overall size of the protein. In fact, about 10 amino acids make

up the active site.

Quiz Score: 90 out of 100