Homework Answers
Role of the glycosyl transferase is to recognize mosfolded glycoprotein and transfer a glucose monomer to terminal mannose,on the glycoprotein.UDP glucose act as glucosyl donor.
if glucosyl transferase interacts with anyprotein regardless of folded and misfolded ,both folded and misfolded protein is monoglucosylated by glucosyl transferase.folded protein also enter in to the cycle of calnexin and calreticulin folding pathway.both protein remain in ER lumen.
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B. Glucosyl transferase is an important enzyme in the calnexin protein folding process. What would happen...
Protein Folding - a) what is the molten globule? b) How does the activity of chaperones...
Protein Folding - a) what is the molten globule? b) How does the activity of chaperones in unfolding molten globules may enhance the overall rate of folding to the native state? c) Name a protein folding disease. d) Give two possible general causes for disease arising from protein folding defects.
For a protein such as ribonuclease, for the process of protein folding under native (non-denaturing) conditions,...
For a protein such as ribonuclease, for the process of protein folding under native (non-denaturing) conditions, Punfolded → Pfolded Select the appropriate description for each of the thermodynamic parameters (for the folding reaction as shown above, from left to right): What is the value of ∆G? What is the value of ∆Sconformational? The value of ∆S hydrophobic? The choices for each question A. positive, favorable for folding B. positive, unfavorable for folding C. negative, favorable for folding D. negative, unfavorable...
this is a very simplistic approach to protein folding which ignores solvent and volume affect but...
this is a very simplistic approach to protein folding
which ignores solvent and volume affect but it allows us to
practice what we have learned about thermodynamics and kinetics.
enzymes are long chains of amino acids that have to fold in the
proper way so as to exhibit enzyme activity. They can get lice or
dandruff reactions. Let us pick an enzyme that is produced in the
human body at 37 degrees Celsius. We will call it enzyme X. Human...
Predict what would happen to the secondary structure of a protein if an alcohol that disrupts...
Predict what would happen to the secondary structure of a protein if an alcohol that disrupts hydrogen bonding were added. Choose one or more answer (if applied): A. Nothing would happen to the protein; hydrogen bonding is not important for secondary structure B. The beta sheets would unfold, disrupting protein structure C. The a helixes would unfold, disrupting protein structure D. Individual amino acids would be hydrolyzed from the protein, disrupting protein structure
QUESTION 1 To study how proteins fold, scientists must be able to purify the protein of...
QUESTION 1 To study how proteins fold, scientists must be able to purify the protein of interest, use solvents like urea to denature the folded protein, and observe the process of refolding at successive time points. What is the effect of the solvents used in the denaturation process? a. The solvents break all noncovalent interactions. b. The solvents break all covalent interactions. c. The solvents create a new folded conformation. d. The solvents break some of the noncovalent interactions, resulting...
a)b) topoisomerase IT As the replication fork continues to open, what will happen to the protein...
a)b)
topoisomerase IT As the replication fork continues to open, what will happen to the protein labeled “C”? Is this the same in prokaryotes and eukaryotes? Briefly explain what would happen if the protein RPA did not come in to perform its function in regards to primers. How will protein C be impacted as a result and why? Is this the same in prokaryotes and eukaryotes?
a) What aspects of protein structure and folding are explained by entropy? How does entropy affect...
a) What aspects of protein structure and folding are explained
by entropy? How does entropy
affect a protein’s native versus denatured structure?
b) What aspects of protein structure and folding are explained
by enthalpy? How does enthalpy
affect a protein’s native versus denatured structure?
c) What aspects of protein structure and folding are
illustrative of equilibrium (or disequilibrium)?
1. The figure below shows the physical representation of a native protein versus a denatured protein 72 native state A-state 23 17...
3. Indicate the (major) class of enzym major class of enzyme that would be required to...
3. Indicate the (major) class of enzym major class of enzyme that would be required to catalyze each of the following reactions. The options include: oxidoreductase, isomerase, transferase, hydrolase, lyase, and ligase. . - 4. Consider the following 31 residue polypeptide N-Terminal 9000 C-Terminal a. Predict how the following denaturants will affect the folded structure of this polypeptide. What specific regions (or attractive forces/covalent linkages) will be affected by each of these reagents? Use the residue numbers to locate particular...
What would happen if the enzyme was non-functional for Polymerase, I Polymerase III, Ligase, Helicase and...
What would happen if the enzyme was non-functional for Polymerase, I Polymerase III, Ligase, Helicase and Okazaki Explain please
3. Discuss the polarity of the lipid bilayer. 4. Explain how protein folding is related to...
3. Discuss the polarity of the lipid bilayer. 4. Explain how protein folding is related to intermolecular forces. 5. Caffeine is a stimulant contained in coffee. Use what you know about polarity to come up with a plan to extract caffeine from coffee. Write down any reagents that you would use.
this is a very simplistic approach to protein folding
which ignores solvent and volume affect but it allows us to
practice what we have learned about thermodynamics and kinetics.
enzymes are long chains of amino acids that have to fold in the
proper way so as to exhibit enzyme activity. They can get lice or
dandruff reactions. Let us pick an enzyme that is produced in the
human body at 37 degrees Celsius. We will call it enzyme X. Human...
a)b)
topoisomerase IT As the replication fork continues to open, what will happen to the protein labeled “C”? Is this the same in prokaryotes and eukaryotes? Briefly explain what would happen if the protein RPA did not come in to perform its function in regards to primers. How will protein C be impacted as a result and why? Is this the same in prokaryotes and eukaryotes?
a) What aspects of protein structure and folding are explained
by entropy? How does entropy
affect a protein’s native versus denatured structure?
b) What aspects of protein structure and folding are explained
by enthalpy? How does enthalpy
affect a protein’s native versus denatured structure?
c) What aspects of protein structure and folding are
illustrative of equilibrium (or disequilibrium)?
1. The figure below shows the physical representation of a native protein versus a denatured protein 72 native state A-state 23 17...
3. Indicate the (major) class of enzym major class of enzyme that would be required to catalyze each of the following reactions. The options include: oxidoreductase, isomerase, transferase, hydrolase, lyase, and ligase. . - 4. Consider the following 31 residue polypeptide N-Terminal 9000 C-Terminal a. Predict how the following denaturants will affect the folded structure of this polypeptide. What specific regions (or attractive forces/covalent linkages) will be affected by each of these reagents? Use the residue numbers to locate particular...
3. Discuss the polarity of the lipid bilayer. 4. Explain how protein folding is related to intermolecular forces. 5. Caffeine is a stimulant contained in coffee. Use what you know about polarity to come up with a plan to extract caffeine from coffee. Write down any reagents that you would use.
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