Question 1

Which of the following amino acids can be phosphorylated?

Accepted Answer

A)  tyrosine, serine, threonine 
B)  tyrosine, serine, tryptophan 
C)  serine, threonine, asparagine 
D)  histidine, serine, phenylalanine 
E)  tyrosine, methionine, tryptophan 
A)  tyrosine, serine, threonine 
B)  tyrosine, serine, tryptophan 
C)  serine, threonine, asparagine 
D)  histidine, serine, phenylalanine 
E)  tyrosine, methionine, tryptophan A

Question 2

Use the following to answer questions
Choose the correct answer from the list below. Not all of the answers will be used.
-The enzyme that becomes active when bound to cAMP is ____________.

Accepted Answer

A) protein kinase A (PK
A)  
B) calmodulin 
C) fatty acids 
D) proto-oncogene 
E) R2C2
F)R1C2
G)cAMP
H)phospholipase C
I)protein kinase C (PK
C) 
J)epinephrine
K)oncogene
L)small G proteins 
A) protein kinase A (PK
A)  
B) calmodulin 
C) fatty acids 
D) proto-oncogene 
E) R2C2
F)R1C2
G)cAMP
H)phospholipase C
I)protein kinase C (PK
C) 
J)epinephrine
K)oncogene
L)small G proteins A

Question 3

Cross-phosphorylation is possible when two receptor proteins with kinase domains:

Accepted Answer

A)  are cleaved. 
B)  form dimers. 
C)  are internalized into organelles. 
D)  All of the above. 
E)  None of the above. 
A)  are cleaved. 
B)  form dimers. 
C)  are internalized into organelles. 
D)  All of the above. 
E)  None of the above. B

Question 4

What is meant by an EF hand? Draw or describe the structure.

Accepted Answer

The EF hand is a protein that binds calc

Question 5

What is the difference between heterotrimeric G proteins and small G proteins?

Accepted Answer

Heterotrimeric G proteins are composed o

Question 6

How many 7TM membranes are there? What are some of their functions?

Accepted Answer

There are estimated to be thousands of 7

Question 7

Which form of the guanyl nucleotide is bound in the unactivated state?

Accepted Answer

A)  GTP 
B)  GDP 
C)  GMP 
D)  dGTP 
E)  None of the above. 
A)  GTP 
B)  GDP 
C)  GMP 
D)  dGTP 
E)  None of the above.

Question 8

How does binding of epinephrine initiate the cAMP production? Discuss briefly in terms of receptor structure and function.

Accepted Answer

Epinephrine binds to a 7TM receptor whic

Question 9

What is a disadvantage of using common molecules for signaling paths?

Accepted Answer

When second messengers are involved in m

Question 10

The ________________ is a calcium-binding unit in many proteins and is characterized by a helix-loop-helix structure.

Accepted Answer

The answer of The ________________ is a calcium-binding unit in...

Question 11

Use the following to answer questions
Choose the correct answer from the list below. Not all of the answers will be used.
-The ____________ protein binds to calcium ions and serves as a Ca2+ sensor in eukaryotic cells.

Accepted Answer

A) protein kinase A (PK
A)  
B) calmodulin 
C) fatty acids 
D) proto-oncogene 
E) R2C2
F)R1C2
G)cAMP
H)phospholipase C
I)protein kinase C (PK
C) 
J)epinephrine
K)oncogene
L)small G proteins 
A) protein kinase A (PK
A)  
B) calmodulin 
C) fatty acids 
D) proto-oncogene 
E) R2C2
F)R1C2
G)cAMP
H)phospholipase C
I)protein kinase C (PK
C) 
J)epinephrine
K)oncogene
L)small G proteins

Question 12

________________ binds to β-andrenergic receptors.

Accepted Answer

Epinephrin

Question 13

Example(s) of disease(s) caused by altered G-protein activity include:

Accepted Answer

A)  whooping cough. 
B)  cholera. 
C)  diabetes. 
D)  A and B. 
E)  B and C. 
A)  whooping cough. 
B)  cholera. 
C)  diabetes. 
D)  A and B. 
E)  B and C.

Question 14

What happens when signaling paths are not terminated properly?

Accepted Answer

The cell will not be able to r

Question 15

The binding of IP3 to the IP3 receptor results in the release of ________________ from the endoplasmic reticulum.

Accepted Answer

The answer of The binding of IP3 to the IP3...

Question 16

Use the following to answer questions
Choose the correct answer from the list below. Not all of the answers will be used.
-____________: The ɑ and subunits of heterotrimeric G proteins are anchored to the cell membrane by being covalently linked to these types of molecule.

Accepted Answer

A) protein kinase A (PK
A)  
B) calmodulin 
C) fatty acids 
D) proto-oncogene 
E) R2C2
F)R1C2
G)cAMP
H)phospholipase C
I)protein kinase C (PK
C) 
J)epinephrine
K)oncogene
L)small G proteins 
A) protein kinase A (PK
A)  
B) calmodulin 
C) fatty acids 
D) proto-oncogene 
E) R2C2
F)R1C2
G)cAMP
H)phospholipase C
I)protein kinase C (PK
C) 
J)epinephrine
K)oncogene
L)small G proteins

Question 17

What are receptor tyrosine kinases? Provide an example.

Accepted Answer

These are proteins that bind l

Question 18

Most signal molecules:

Accepted Answer

A)  easily diffuse through the membrane and bind to a receptor in the cytoplasm. 
B)  bind to membrane receptors and transmit information across a membrane without traversing the membrane. 
C)  carry out functions in the nucleus after binding to a receptor in the cell membrane. 
D)  A and C. 
E)  A, B, and C. 
A)  easily diffuse through the membrane and bind to a receptor in the cytoplasm. 
B)  bind to membrane receptors and transmit information across a membrane without traversing the membrane. 
C)  carry out functions in the nucleus after binding to a receptor in the cell membrane. 
D)  A and C. 
E)  A, B, and C.

Question 19

Why is bound GTP considered a "clock"?

Accepted Answer

A)  It behaves in specific time intervals. 
B)  GTP is exchanged for GDP after binding to adenylate cyclase. 
C)  The Gɑ receptors have intrinsic GTPase activity, hydrolyzing GTP to GDP and Pi. 
D)  All of the above. 
E)  None of the above. 
A)  It behaves in specific time intervals. 
B)  GTP is exchanged for GDP after binding to adenylate cyclase. 
C)  The Gɑ receptors have intrinsic GTPase activity, hydrolyzing GTP to GDP and Pi. 
D)  All of the above. 
E)  None of the above.

Question 20

The cytosolic side, or β subunit, of the insulin receptor is a ________________ kinase.

Accepted Answer

The answer of The cytosolic side, or β subunit, of...

Exam 13: Signal Transduction Pathways

Which of the following amino acids can be phosphorylated?

Use the following to answer questions Choose the correct answer from the list below. Not all of the answers will be used. -The enzyme that becomes active when bound to cAMP is ____________.

Cross-phosphorylation is possible when two receptor proteins with kinase domains:

What is meant by an EF hand? Draw or describe the structure.

What is the difference between heterotrimeric G proteins and small G proteins?

How many 7TM membranes are there? What are some of their functions?

Which form of the guanyl nucleotide is bound in the unactivated state?

How does binding of epinephrine initiate the cAMP production? Discuss briefly in terms of receptor structure and function.

What is a disadvantage of using common molecules for signaling paths?

The ________________ is a calcium-binding unit in many proteins and is characterized by a helix-loop-helix structure.

Use the following to answer questions Choose the correct answer from the list below. Not all of the answers will be used. -The ____________ protein binds to calcium ions and serves as a Ca2+ sensor in eukaryotic cells.

________________ binds to β-andrenergic receptors.

Example(s) of disease(s) caused by altered G-protein activity include:

What happens when signaling paths are not terminated properly?

The binding of IP3 to the IP3 receptor results in the release of ________________ from the endoplasmic reticulum.

Use the following to answer questions Choose the correct answer from the list below. Not all of the answers will be used. -____________: The ɑ and subunits of heterotrimeric G proteins are anchored to the cell membrane by being covalently linked to these types of molecule.

What are receptor tyrosine kinases? Provide an example.

Most signal molecules:

Why is bound GTP considered a "clock"?

The cytosolic side, or β subunit, of the insulin receptor is a ________________ kinase.

Biochemistry and the Unity of Life

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

Amino Acids

Protein Three-Dimensional Structure

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

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