Question 1

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.

Question 2

What causes this latency?

Accepted Answer

Prion diseases are protein based; more s

Question 3

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 4

The configuration of most α-carbon atoms of amino acids linked in a peptide bond is:

Accepted Answer

A)  cis. 
B)  circular. 
C)  parallel. 
D)  trans. 
E)  perpendicular. 
A)  cis. 
B)  circular. 
C)  parallel. 
D)  trans. 
E)  perpendicular.

Question 5

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

Accepted Answer

If some regions interact prefe

Question 6

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 7

Choose the correct answer from the list below. Not all of the answers will be used.
-According to convention, ____________ is the terminus drawn on the left side of a peptide.

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 8

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 9

Where are Ω and β turns and loops often found?

Accepted Answer

A)  in a hydrophobic pocket 
B)  on the interior cleft 
C)  at the protein interface with ligand 
D)  on the surface of proteins 
E)  None of the above. 
A)  in a hydrophobic pocket 
B)  on the interior cleft 
C)  at the protein interface with ligand 
D)  on the surface of proteins 
E)  None of the above.

Question 10

What is the advantage of protein interaction and assembly with other proteins?

Accepted Answer

When proteins interact or assemble, new

Exam 4: Protein Three-Dimensional Structure

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

What causes this latency?

Key properties of proteins include:

The configuration of most α-carbon atoms of amino acids linked in a peptide bond is:

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

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.

Choose the correct answer from the list below. Not all of the answers will be used. -According to convention, ____________ is the terminus drawn on the left side of a peptide.

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.

Where are Ω and β turns and loops often found?

What is the advantage of protein interaction and assembly with other proteins?

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