what changes occur in the structure of a protein molecule when it becomes denatured
what changes occur in the structure of a protein molecule when it becomes denatured
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what changes occur in the structure of a protein
molecule when it becomes denatured
question 3: what happens to the structure of a protein when it is denatured? question 4:...
question 3: what happens to the structure of a protein when it is
denatured?
question 4: why is it important for a protein to be at a
certain ph to carry out its function
zymes in your textbook, especially the sections on enzym REPORT: Your report should include two separate files: a table of the data from your enzyme experiments online and conclusions consisting of answers to the questions. WARM-UP QUESTIONS: 1. What part of the name 6-O-a-L-ramnosyl-D-glucosidase shows that...
3. Thermodynamies of protein folding. The native and denatured forms of a protein are generally in...
3. Thermodynamies of protein folding. The native and denatured forms of a protein are generally in equilibrium. Protein (denatured) Protein (native) For a certain solution of the protein ribonuclease A, in which the total protein concentration is 2.0 x 10 M, the concentrations of the denatured and native proteins at 50 and 100°C are listed below. Protein (denatureの S.I x 10M 2.8 x 10 M Protein (native) 2.0 x 10 MM 1.7 x 10M Temperature 50°C 100°C lding reaction. [Assume...
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...
The native and denatured forms of a protein are generally in equilibrium. For a certain solution...
The native and denatured forms of a protein are generally in equilibrium. For a certain solution of the protein ribonuclease A, in which the total protein concentration is 2.0 x 10^-3 M, the H concentrations of the denatured and native proteins at 50 and 100degreeC are listed below. Determine AS and AH for the folding reaction. [Asinine these quantities are independent of temperature.] Calculate deltaG degree for ribonuclease A folding at 25degreeC. Is this reaction spontaneous at this temperature? What...
Is it true that the more resonance structure a molecule has, the less polar it becomes?
Is it true that the more resonance structure a molecule has, the less polar it becomes?
. Consider a flexible (random-walk) polymer description of a protein in its denatured state. The ...
. Consider a flexible (random-walk) polymer description of a protein in its denatured state. The protein chain consists of 300 amino-acids, and the separation between the C atoms of each amino-acid is 0.36 nm. The statistical segment length of an unfolded protein contains about 6 amino-acids. (a) How many statistically independent segments are there in this unfolded protein chain? (b) What is the size (root-mean-square end-to-end distance) of the unfolded protein? (c) What is its entropic spring constant?
. Consider...
1st attempt See Hint When a protein folds, transitioning from denatured to native state, the change...
1st attempt See Hint When a protein folds, transitioning from denatured to native state, the change in free energy is favorable (AG<0). In general, the entropic change is (A) due to the more limited number of conformations. The enthalpic change is (B) due to the many weak interactions that are formed. With the exception of disulfide bonds, weak interactions include the formation of (C) and numerous (D) . in the native state.
lation stops when the ribosome A) Runs into a repressor protein B) Becomes stuck on an...
lation stops when the ribosome A) Runs into a repressor protein B) Becomes stuck on an operator sequence c) Reaches a stop codorn D) All of the above E) B and C 28) The numerical notation for the correct reading frame i.... A) 0 B) 1 C) -1 D) +1 E) -10 29) What is the role(s) of chaperone proteins (chaperonins)? A) They assist the ribosome in binding to the beginning of mRNA. B) They properly fold nascent proteins into...
biochem quest. Each of the following reagents or conditions will denature a protein. For each, describe what the re...
biochem quest.
Each of the following reagents or conditions will denature a protein. For each, describe what the reagent/condition does to interrupt the native protein structure. (a) temperature (c) detergent (d) extreme pH. Show a melting curve ofa protein - label the Tm and indicate on your graph whether the protein is found in its native structure or in a denatured state. (8 points) (b) high urea
Each of the following reagents or conditions will denature a protein. For each,...
What are two major types of protein secondary structure, and what kind of interaction holds them...
What are two major types of protein secondary structure, and what kind of interaction holds them together , and between what part of the protein do they occur?
question 3: what happens to the structure of a protein when it is
denatured?
question 4: why is it important for a protein to be at a
certain ph to carry out its function
zymes in your textbook, especially the sections on enzym REPORT: Your report should include two separate files: a table of the data from your enzyme experiments online and conclusions consisting of answers to the questions. WARM-UP QUESTIONS: 1. What part of the name 6-O-a-L-ramnosyl-D-glucosidase shows that...
3. Thermodynamies of protein folding. The native and denatured forms of a protein are generally in equilibrium. Protein (denatured) Protein (native) For a certain solution of the protein ribonuclease A, in which the total protein concentration is 2.0 x 10 M, the concentrations of the denatured and native proteins at 50 and 100°C are listed below. Protein (denatureの S.I x 10M 2.8 x 10 M Protein (native) 2.0 x 10 MM 1.7 x 10M Temperature 50°C 100°C lding reaction. [Assume...
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...
The native and denatured forms of a protein are generally in equilibrium. For a certain solution of the protein ribonuclease A, in which the total protein concentration is 2.0 x 10^-3 M, the H concentrations of the denatured and native proteins at 50 and 100degreeC are listed below. Determine AS and AH for the folding reaction. [Asinine these quantities are independent of temperature.] Calculate deltaG degree for ribonuclease A folding at 25degreeC. Is this reaction spontaneous at this temperature? What...
. Consider a flexible (random-walk) polymer description of a protein in its denatured state. The protein chain consists of 300 amino-acids, and the separation between the C atoms of each amino-acid is 0.36 nm. The statistical segment length of an unfolded protein contains about 6 amino-acids. (a) How many statistically independent segments are there in this unfolded protein chain? (b) What is the size (root-mean-square end-to-end distance) of the unfolded protein? (c) What is its entropic spring constant?
. Consider...
1st attempt See Hint When a protein folds, transitioning from denatured to native state, the change in free energy is favorable (AG<0). In general, the entropic change is (A) due to the more limited number of conformations. The enthalpic change is (B) due to the many weak interactions that are formed. With the exception of disulfide bonds, weak interactions include the formation of (C) and numerous (D) . in the native state.
lation stops when the ribosome A) Runs into a repressor protein B) Becomes stuck on an operator sequence c) Reaches a stop codorn D) All of the above E) B and C 28) The numerical notation for the correct reading frame i.... A) 0 B) 1 C) -1 D) +1 E) -10 29) What is the role(s) of chaperone proteins (chaperonins)? A) They assist the ribosome in binding to the beginning of mRNA. B) They properly fold nascent proteins into...
biochem quest.
Each of the following reagents or conditions will denature a protein. For each, describe what the reagent/condition does to interrupt the native protein structure. (a) temperature (c) detergent (d) extreme pH. Show a melting curve ofa protein - label the Tm and indicate on your graph whether the protein is found in its native structure or in a denatured state. (8 points) (b) high urea
Each of the following reagents or conditions will denature a protein. For each,...
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