Homework Answers
"Polypeptide"
the synthesis polypeptide chain with a sequence of amino acid must fold into distinct three-dimensional conformations, and in many cases, multiple polypeptide chains must assemble into a functional complex. These types of synthesize protein to provide an environment to ensure protein folding and proper conformation.
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This protein is synthesized to provide an environment to ensure protein folding and proper conformation.
How does the hydrophobic effect influence protein folding? In an aqueous environment, nonpolar portions of the...
How does the hydrophobic effect influence protein folding? In an aqueous environment, nonpolar portions of the molecule A) are generally exposed to solvent and interact effectively with water. B) interact with polar portions in the interior of the protein. C) can be placed on the surface of the molecule only if hydrogen bonded to water. D) are found in the interior of the protein, away from water, which preserves the entropy of water in solution.
10. Protein folding, in most cases, is complex and inhibited by aggregation. Which of the following...
10. Protein folding, in most cases, is complex and inhibited by aggregation. Which of the following is false regarding protein folding? A. Chaperones of the heat shock classes do not promote folding, but rather inhibit aggregation. B. Enzymes promote the formation of proper disulfide linkages by eliminating improper folding. C. All proteins require the input of energy and the assistance of chaperones for folding. D. Secondary structures usually form first in folding.
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...
. The equilibrium constant for folding of a protein at a certain temperature is Keq =...
. The equilibrium constant for folding of a protein at a certain temperature is Keq = 14.0. The relaxation time at the same temperature is τrelax = 0.233 sec. Compute the folding and unfolding rate constants of this protein at this temperature. 12 pts
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.
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...
Which of these is an example of secondary protein structure? folding pattern of individual amino acid...
Which of these is an example of secondary protein structure? folding pattern of individual amino acid chains sequence of amino acids folding pattern of the protein as a whole combination of amino acid chains in a protein
The native conformation of a protein: 1- is found only when the protein is first formed,...
The native conformation of a protein: 1- is found only when the protein is first formed, but not afterwards. 2- none of the other answers are true. 3- has biological activity 4- is any possible conformation of the protein
1. How can protein folding affect protein function? 2. How can amino acid sequence affect protein...
1. How can protein folding affect protein function? 2. How can amino acid sequence affect protein function? 3. How can an amino acid sequence (primary sequence) dictate 3D protein structure?
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...
10. Protein folding, in most cases, is complex and inhibited by aggregation. Which of the following is false regarding protein folding? A. Chaperones of the heat shock classes do not promote folding, but rather inhibit aggregation. B. Enzymes promote the formation of proper disulfide linkages by eliminating improper folding. C. All proteins require the input of energy and the assistance of chaperones for folding. D. Secondary structures usually form first in folding.
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...
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