Protein S will fold into its native conformation only when protein Q is also present in...
Protein S will fold into its native conformation only when protein Q is also present in the solution. However, protein Q can fold into its native conformation without protein S. What is the most likely explanation. Briefly explain in 1-4 sentences.
Homework Answers
Protein Q can be molecular chaperone . Molecular chaperones are the proteins that help in covalent folding or unfolding of large proteins. Molecular chaperones are heat shock proteins which are expressed under heat shocks . They are expressed under heat shock because high heat may affect the protein folding of many proteins, then molecular chaperones may prevent this misfolding or correct the damage in misfolding.
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Protein S will fold into its native conformation only when
protein Q is also present in...
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
please help with these 4 questions and explain why you chose what you did. thanks and...
please help with these 4 questions and explain why you
chose what you did. thanks and I'll give thumbs up.
11. A particular amino acid without an ionizable R-group would have a pl of is 3.1 and pK2 is 8.9 ; if its pK1 2.9 a. b. 5.8 6 C. d. 12 12. A certain amino acid with an ionizable side chain has a pK1 of 2.4, a pK2 of 8.9, and a pKR of 6.5. If the amino acid...
5. The hypothetical protein E contains no tyrosine residues and 3 tryptophan residues. When in the...
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Suppose you have a protein that can assume four possible conformations (A,B,C,D). When prepared, the protein...
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(a) Into which channel is Fe2+ most likely to travel? Briefly explain your answer by including...
(a) Into which channel is Fe2+ most likely to travel? Briefly
explain your answer by including the dominant interparticle force
between it and the amino acid R groups that line the channel.
(b) Into which channel is O2 most likely to travel? Briefly
explain your answer by including the dominant interparticle force
between it and the amino acid R groups that line the channel.
(c) Suppose there is a region in a protein where a significant
amount of H bonding...
SULR as the fow thermometer un 2. When a protein denatures in a cell, what causes...
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17) Consider the following experimental methods that are commonly used in biochemistry: A) dynamic light scattering....
17) Consider the following experimental methods that are commonly used in biochemistry: A) dynamic light scattering. B) polycrylamide gel electrophoresis (PAGE) with SDS present. C) polycrylamide gel electrophoresis (PAGE) without SDS present. D) surface plasmon resonance (SPR) E) differential scanning fluorimetry (DSF) F) analytical ultracentrifugation (equilibrium type) G) gel filtration chromatography (a) Which three of the methods are best for providing an estimate of the molecular weight of a protein in solution, in its native (non-denatured) form? (3 pts) Write...
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3. (2 points) In the nematode roundworm, Caenorhabditis elegans, the LIN-14 protein controls the timing of...
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please help with these 4 questions and explain why you
chose what you did. thanks and I'll give thumbs up.
11. A particular amino acid without an ionizable R-group would have a pl of is 3.1 and pK2 is 8.9 ; if its pK1 2.9 a. b. 5.8 6 C. d. 12 12. A certain amino acid with an ionizable side chain has a pK1 of 2.4, a pK2 of 8.9, and a pKR of 6.5. If the amino acid...
You are working with a protein, which is known to exist in an open (O), partially open (P) and closed conformation (C). The closed state is the functional state of the protein. The energy of the three states are Ec--7 kcal/mol, EP -5 kcal/mol and Eo--4 kcal/mol. a) What is the average energy of this protein at 300 K, assuming constant volume? b) Through mutagenesis experiments you have been trying to identity a version of the protein which stabilizes the...
(a) Into which channel is Fe2+ most likely to travel? Briefly
explain your answer by including the dominant interparticle force
between it and the amino acid R groups that line the channel.
(b) Into which channel is O2 most likely to travel? Briefly
explain your answer by including the dominant interparticle force
between it and the amino acid R groups that line the channel.
(c) Suppose there is a region in a protein where a significant
amount of H bonding...
SULR as the fow thermometer un 2. When a protein denatures in a cell, what causes it to aggregate with other denatured cell proteins? (2pts) 3. How might a heat shock protein help a protein fold correctly in a cell under normal conditions? (2 pts). 4. The bacterial GroEL heat-shock protein and the plant Rubisco assembly proteins are said to be homologous proteins. What is it about these proteins that has caused them to be described as members of the...
17) Consider the following experimental methods that are commonly used in biochemistry: A) dynamic light scattering. B) polycrylamide gel electrophoresis (PAGE) with SDS present. C) polycrylamide gel electrophoresis (PAGE) without SDS present. D) surface plasmon resonance (SPR) E) differential scanning fluorimetry (DSF) F) analytical ultracentrifugation (equilibrium type) G) gel filtration chromatography (a) Which three of the methods are best for providing an estimate of the molecular weight of a protein in solution, in its native (non-denatured) form? (3 pts) Write...
3. (2 points) In the nematode roundworm, Caenorhabditis elegans, the LIN-14 protein controls the timing of certain cell divisions during development. LIN-14 protein levels are normally high in early development but decrease in the later stages. In a lin-4 mutant, the level of LIN-14 protein stays high throughout development, changing the pattern of cell divisions in the animal and producing defects in the shape of the animal. The lin-4 gene encodes a microRNA that binds to a sequence in the...
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