Question 1

Prion diseases are often latent; that is, those with prion diseases are asymptomatic for many years after their initial infection. What causes this latency?

Accepted Answer

Prion diseases are protein based; more s

Question 2

What is the sequence of amino acids found in collagen? What is the significance of the sequence and what is the complication of scurvy?

Accepted Answer

Gly-Pro-Pro. The small side group of the

Question 3

How does the protein backbone add to structural stability?

Accepted Answer

The protein backbone contains the peptid

Question 4

Why are all the theoretical combinations of phi and psi not possible?

Accepted Answer

Steric hindrances of

Question 5

_______________ is a fibrous protein and is the primary component of wool and hair.

Accepted Answer

The answer of _______________ is a fibrous protein and is...

Question 6

Collagen contains _______________, a modified amino acid.

Accepted Answer

The answer of Collagen contains _______________, a modified amino acid....

Question 7

The _______________ indicates the left- or right-handedness of an alpha helix.

Accepted Answer

The answer of The _______________ indicates the left- or right-handedness...

Question 8

Use the following to answer questions
Choose the correct answer from the list below. Not all of the answers will be used.
-____________: Codes for the sequence of amino acids.

Accepted Answer

A) amino 
B) water 
C) protons 
D) DNA 
E) secondary structure
F)tertiary structure
G)Ramachandran
H)RNA
I)domain
J)cystine
K)proline
L)Sanger
M)D amino acids
N)cysteine 
A) amino 
B) water 
C) protons 
D) DNA 
E) secondary structure
F)tertiary structure
G)Ramachandran
H)RNA
I)domain
J)cystine
K)proline
L)Sanger
M)D amino acids
N)cysteine

Question 9

The _______________ β-sheet structure occurs when the two strands are oriented in opposite directions (N →
C).

Accepted Answer

The answer of The _______________ β-sheet structure occurs when the...

Question 10

Why is the peptide bond planar?

Accepted Answer

A)  Bulky side chains prevent free rotation around the bond. 
B)  It exhibits partial double-bond character, preventing rotation. 
C)  Hydrogen bonding between the NH and C=O groups limits movement. 
D)  None of the above. 
E)  All of the above. 
A)  Bulky side chains prevent free rotation around the bond. 
B)  It exhibits partial double-bond character, preventing rotation. 
C)  Hydrogen bonding between the NH and C=O groups limits movement. 
D)  None of the above. 
E)  All of the above.

Question 11

_______________ refers to the spatial arrangement of subunits and the nature of their interactions.

Accepted Answer

Quaternary

Question 12

What is the advantage of having certain regions of partially correct folded regions?

Accepted Answer

If some regions interact prefe

Question 13

Which of the following amino acid residues would most likely be buried in the interior of a water-soluble, globular protein?

Accepted Answer

A)  Aspartate 
B)  Serine 
C)  Phenylalanine 
D)  Lysine 
E)  Glutamine 
A)  Aspartate 
B)  Serine 
C)  Phenylalanine 
D)  Lysine 
E)  Glutamine

Question 14

The secondary structure that is stabilized by CO and NH hydrogen bonding within the peptide chain is the _______________.

Accepted Answer

The answer of The secondary structure that is stabilized by...

Question 15

Due to the side group steric clash, almost all peptide bonds are _______________ in their configuration.

Accepted Answer

The answer of Due to the side group steric clash,...

Question 16

A protein is considered to be _______________ when it is converted into a randomly coiled structure without its normal activity.

Accepted Answer

The answer of A protein is considered to be _______________...

Question 17

Use the following to answer questions
Choose the correct answer from the list below. Not all of the answers will be used.
-____________: This amino acid residue disrupts the α helix because its side chain contains a unique ring structure that restricts bond rotations.

Accepted Answer

A) amino 
B) water 
C) protons 
D) DNA 
E) secondary structure
F)tertiary structure
G)Ramachandran
H)RNA
I)domain
J)cystine
K)proline
L)Sanger
M)D amino acids
N)cysteine 
A) amino 
B) water 
C) protons 
D) DNA 
E) secondary structure
F)tertiary structure
G)Ramachandran
H)RNA
I)domain
J)cystine
K)proline
L)Sanger
M)D amino acids
N)cysteine

Question 18

Use the following to answer questions
Choose the correct answer from the list below. Not all of the answers will be used.
-____________: The type of structure to which α helices, β sheets, and turns are referred.

Accepted Answer

A) amino 
B) water 
C) protons 
D) DNA 
E) secondary structure
F)tertiary structure
G)Ramachandran
H)RNA
I)domain
J)cystine
K)proline
L)Sanger
M)D amino acids
N)cysteine 
A) amino 
B) water 
C) protons 
D) DNA 
E) secondary structure
F)tertiary structure
G)Ramachandran
H)RNA
I)domain
J)cystine
K)proline
L)Sanger
M)D amino acids
N)cysteine

Question 19

Key properties of proteins include:

Accepted Answer

A)  a wide range of functional groups. 
B)  an ability to possess either rigid or flexible structures as dictated by functional requirements. 
C)  the ability to interact with other proteins. 
D)  A and B. 
E)  All of the above. 
A)  a wide range of functional groups. 
B)  an ability to possess either rigid or flexible structures as dictated by functional requirements. 
C)  the ability to interact with other proteins. 
D)  A and B. 
E)  All of the above.

Question 20

What is the approximate mass of a protein containing 200 amino acids? (Assume there are no other protein modifications.)

Accepted Answer

A)  20,000 
B)  11,000 
C)  22,000 
D)  222,000 
E)  None of the above. 
A)  20,000 
B)  11,000 
C)  22,000 
D)  222,000 
E)  None of the above.

Exam 4: Protein Three-Dimensional Structure

Prion diseases are often latent; that is, those with prion diseases are asymptomatic for many years after their initial infection. What causes this latency?

What is the sequence of amino acids found in collagen? What is the significance of the sequence and what is the complication of scurvy?

How does the protein backbone add to structural stability?

Why are all the theoretical combinations of phi and psi not possible?

_______________ is a fibrous protein and is the primary component of wool and hair.

Collagen contains _______________, a modified amino acid.

The _______________ indicates the left- or right-handedness of an alpha helix.

Use the following to answer questions Choose the correct answer from the list below. Not all of the answers will be used. -____________: Codes for the sequence of amino acids.

The _______________ β-sheet structure occurs when the two strands are oriented in opposite directions (N → C).

Why is the peptide bond planar?

_______________ refers to the spatial arrangement of subunits and the nature of their interactions.

What is the advantage of having certain regions of partially correct folded regions?

Which of the following amino acid residues would most likely be buried in the interior of a water-soluble, globular protein?

The secondary structure that is stabilized by CO and NH hydrogen bonding within the peptide chain is the _______________.

Due to the side group steric clash, almost all peptide bonds are _______________ in their configuration.

A protein is considered to be _______________ when it is converted into a randomly coiled structure without its normal activity.

Use the following to answer questions Choose the correct answer from the list below. Not all of the answers will be used. -____________: This amino acid residue disrupts the α helix because its side chain contains a unique ring structure that restricts bond rotations.

Use the following to answer questions Choose the correct answer from the list below. Not all of the answers will be used. -____________: The type of structure to which α helices, β sheets, and turns are referred.

Key properties of proteins include:

What is the approximate mass of a protein containing 200 amino acids? (Assume there are no other protein modifications.)

Biochemistry and the Unity of Life

Water, Weak Bonds, and the Generation of Order Out of Chaos

Amino Acids

Techniques in Protein Biochemistry

Basic Concepts of Enzyme Action

Kinetics and Regulation

Mechanisms and Inhibitors

Hemoglobin: an Allosteric Protein

Carbohydrates

Lipids

Membrane Structure and Function

Signal Transduction Pathways

Digestion: Turning a Meal Into Cellular Biochemicals

Metabolism: Basic Concepts and Design

Glycolysis

Gluconeogenesis

Preparation for the Cycle

Harvesting Electrons From the Cycle

The Electron Transport Chain

The Proton-Motive Force

The Light Reactions

The Calvin Cycle

Glycogen Degradation

Glycogen Synthesis

The Pentose Phosphate Pathway

Fatty Acid Degredation

Fatty Acid Synthesis

Lipid Synthesis

Amino Acid Degradation and the Urea Cycle

Amino Acids Synthesis

Nucleotide Metabolism

The Structure of Informational Macromolecules: Dna and Rna

DNA Replication

DNA Repair and Recombination

RNA Synthesis and Regulation in Prokaryotes

Gene Expression in Eukaryotes

RNA Processing in Eukaryotes

The Genetic Code

The Mechanism of Protein Synthesis

Recombinant Dna Techniques

Filters