Which of these proteins assumes a quaternary structure in its biochemically active state? Chymotrypsin Elastase Hemoglobin...
Which of these proteins assumes a quaternary structure in its biochemically active state?
Chymotrypsin
Elastase
Hemoglobin
None of these
Homework Answers
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Which of these proteins assumes a quaternary structure in its
biochemically active state?
Chymotrypsin
Elastase
Hemoglobin...
Which of the following is an example of a protein that exhibits a quaternary structure?
16) Which of the following is an example of a protein that exhibits a quaternary structure? 1. a) insulin 2. b) hemoglobin 3.c) collagen 4. d) keratin 2 4 3 1 Question 3 3) The a-helix and ß-pleated sheet are both forms of the structure of proteins. a) primary b) secondary c) tertiary d) quaternary
The structure of the active site of chymotrypsin is shown below. The catalytic triad shown (Ser...
The structure of the active site of chymotrypsin is shown below. The catalytic triad shown (Ser 195, His 57, and aspl02) are shown. A peptide with a phenylalanine is shown bound in the active site. 1. Chymotrypsin is a serine protease. The Km for chymotrypsin with N-acetylvaline ethyl ester is 8.8 X 102 M. The Km for the reaction with N-acetyltyrosine ethyl ester is 6.6 X 10 (a) Which substrate has the higher affinity for this enzyme? (b) Give a...
Respiratory alkalosis leads to a shift of hemoglobin to the active R state. At first, it...
Respiratory alkalosis leads to a shift of hemoglobin to the active R state. At first, it may be unclear why shifting to the R state is a bad thing, but the reason should be clear shortly. First, let us examine how CO, also affects hemoglobin directly. CO2 has a direct effect on hemoglobin In addition to its indirect effect on hemoglobin structure through its effect on pH, CO, also directly affects hemoglobin by reacting with the amino-terminal residue of each...
1. Compare and contrast the structure and function of myoglobin to hemoglobin. Provide detailed information & figur...
1. Compare and contrast the structure and function of
myoglobin to hemoglobin. Provide detailed information & figures
on the primary, secondary, tertiary & quarternary structures pf
these proteins, and how these structures reate to function.
2. Provide a detailed drawing (with figures) of the prosthetic
group Heme and a detailed explanation of its role in myoglobin amd
hemoglobin function.
3. Provide a detailed drawing (with figures) of the
cooperative binding of oxygen by hemoglobin.
4. Provide a detailed drawing (with...
UESTION 18 Which one is not an example of a protein with quaternary structure? O A...
UESTION 18 Which one is not an example of a protein with quaternary structure? O A Hemoglobin in adult humans has the composition 02B2 The hemoglobin in sickle cell anemia sufferers has the composition a2S2 OB. Calmodulin is a calcium-binding protein found in eukaryotic organisms. It has two identical subunits OC. Lysozyme, an enzyme that catalyzes the destruction of the cell walls of certain bacteria, consists of a single polypeptide. OD. In plants and some bacteria, the photosynthetic enzyme Rubisco...
With respect to proteins, a change in pH cannot alter: primary structure All of the above...
With respect to proteins, a change in pH cannot alter: primary structure All of the above quaternary structure tertiary structure secondary structure Which of the following statements about phospholipid molecules is false? None of the above phospholipases can switch the acyl groups as well as the head groups have different head groups have glycerol backbone should have palmitate as one of the acyl groups
Heme is the iron-containing structure in the proteins hemoglobin and myoglobin. In red blood cells, hemoglobin...
Heme is the iron-containing structure in the proteins hemoglobin and myoglobin. In red blood cells, hemoglobin enables oxygen uptake and transport. Myoglobin in muscle cells helps oxygen enter the cells. The oxygen carried by hemoglobin and myoglobin is critical for energy production. Because meat contains hemoglobin and myoglobin, beef, fish, and poultry contain more heme iron than most plant foods. The remaining iron in meat, as well as all the iron in vegetables, grains, dietary supplements, and fortified or enriched...
The quaternary structure of ovalbumin D Question 28 2 pts Denaturation, a process in which a...
The quaternary structure of ovalbumin D Question 28 2 pts Denaturation, a process in which a protein loses its native shape and function, is likely to be caused by all of the following except being transported from one cell to another in a living organism. pH change. temperature change. ionic concentration change. increase in hydrogen ion concentration. 2 pts Question 29
20 Marks) Question 3 a) The structure of proteins is described at four levels: primary, secondary,...
20 Marks) Question 3 a) The structure of proteins is described at four levels: primary, secondary, tertiary and quaternary Briefly explain what is referred to by each of these terms. Why are these distinctions useful? [5 marks] b) Each level of protein structure is stabilised by chemical bonds and interactions: List the bonds and/or effects primarily responsible for stabilising each level of structure. [5 marks] c) The illustration below shows a molecule of haemoglobin. Describe TWO (2) aspects of haemoglobin...
#9 quaternary structure. d. This kinetic plot implies that compound "Y" is an activator of this...
#9
quaternary structure. d. This kinetic plot implies that compound "Y" is an activator of this "Michaelis Menten" enzyme. e. Compound "X" binds to a regulatory site on the enzyme 02 and "shifts" the equilibrium to the more active "R" form. 8. Consider the Lineweaver Burk plot of an inhibition experiment of procaine esterase. Which of the following is correct concerning the information indicated by this information? The inhihitor can complex a. n. 6) The KM value is smaller in...
The structure of the active site of chymotrypsin is shown below. The catalytic triad shown (Ser 195, His 57, and aspl02) are shown. A peptide with a phenylalanine is shown bound in the active site. 1. Chymotrypsin is a serine protease. The Km for chymotrypsin with N-acetylvaline ethyl ester is 8.8 X 102 M. The Km for the reaction with N-acetyltyrosine ethyl ester is 6.6 X 10 (a) Which substrate has the higher affinity for this enzyme? (b) Give a...
Respiratory alkalosis leads to a shift of hemoglobin to the active R state. At first, it may be unclear why shifting to the R state is a bad thing, but the reason should be clear shortly. First, let us examine how CO, also affects hemoglobin directly. CO2 has a direct effect on hemoglobin In addition to its indirect effect on hemoglobin structure through its effect on pH, CO, also directly affects hemoglobin by reacting with the amino-terminal residue of each...
1. Compare and contrast the structure and function of
myoglobin to hemoglobin. Provide detailed information & figures
on the primary, secondary, tertiary & quarternary structures pf
these proteins, and how these structures reate to function.
2. Provide a detailed drawing (with figures) of the prosthetic
group Heme and a detailed explanation of its role in myoglobin amd
hemoglobin function.
3. Provide a detailed drawing (with figures) of the
cooperative binding of oxygen by hemoglobin.
4. Provide a detailed drawing (with...
UESTION 18 Which one is not an example of a protein with quaternary structure? O A Hemoglobin in adult humans has the composition 02B2 The hemoglobin in sickle cell anemia sufferers has the composition a2S2 OB. Calmodulin is a calcium-binding protein found in eukaryotic organisms. It has two identical subunits OC. Lysozyme, an enzyme that catalyzes the destruction of the cell walls of certain bacteria, consists of a single polypeptide. OD. In plants and some bacteria, the photosynthetic enzyme Rubisco...
The quaternary structure of ovalbumin D Question 28 2 pts Denaturation, a process in which a protein loses its native shape and function, is likely to be caused by all of the following except being transported from one cell to another in a living organism. pH change. temperature change. ionic concentration change. increase in hydrogen ion concentration. 2 pts Question 29
20 Marks) Question 3 a) The structure of proteins is described at four levels: primary, secondary, tertiary and quaternary Briefly explain what is referred to by each of these terms. Why are these distinctions useful? [5 marks] b) Each level of protein structure is stabilised by chemical bonds and interactions: List the bonds and/or effects primarily responsible for stabilising each level of structure. [5 marks] c) The illustration below shows a molecule of haemoglobin. Describe TWO (2) aspects of haemoglobin...
#9
quaternary structure. d. This kinetic plot implies that compound "Y" is an activator of this "Michaelis Menten" enzyme. e. Compound "X" binds to a regulatory site on the enzyme 02 and "shifts" the equilibrium to the more active "R" form. 8. Consider the Lineweaver Burk plot of an inhibition experiment of procaine esterase. Which of the following is correct concerning the information indicated by this information? The inhihitor can complex a. n. 6) The KM value is smaller in...
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