Answer:
1. more
2. less
3. more
4. less
Explanation:
Consider the reaction: NaNO3(s) + H2SO4(l) NaHSO4(s) + HNO3(g) ΔH° = 21.2 kJ
How much heat must absorbed by the reaction system to convert 100g of NaNO3 into NaHSO4(s)?
Answer:
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When a marble is dropped into a beamer of water
Answer:
The water will rise.Explanation:
hope this helps you
-Sweety<3The mass of the marble is greater than that of the water. The marble weighs more than an equivalent volume of the water. The force from dropping the marble breaks the surface tension of the water. The marble has greater mass and volume than the water.
What volume of each solution contains 0.14 mol of KCl? Express your answer using two significant figures.
1.8 M KCl
Answer:
Solution given:
1 mole of KCl[tex]\rightarrow [/tex]22.4l
1 mole of KCl[tex]\rightarrow [/tex]74.55g
we have
0.14 mole of KCl[tex]\rightarrow [/tex]74.55*0.14=10.347g
74.55g of KCl[tex]\rightarrow [/tex]22.4l
10.347 g of KCl[tex]\rightarrow [/tex]22.4/74.55*10.347=3.11litre
volume of each solution contains 0.14 mol of KCl contain 3.11litre.
[tex]\:[/tex]
1 mole of KCl → 22.4l
1 mole of KCl → 74.55g
we have
0.14 mole of KCl → 74.55*0.14=10.347g
74.55g of KCl → 22.4l
10.347 g of KCl → 22.4/74.55*10.347=3.11litre
volume of each solution contains 0.14 mol of KCl contain 3.11litre.
What is the molecular geometry of CIO3F as predicted by the VSEPR model?
Multiple Choice
trigonal pyramidal
square planar
square pyramidal
tetrahedral
octahedral
Explanation:
since there are no lone pairs on the central atom, the shape will be tetrahedral
Tick (√) the statements that are correct.
a) By eating rice alone, we can fulfil nutritional requirement of our body. ( )
b) Deficiency Diseases can be prevented by eating a balanced diet. ( )
c) Balanced diet for the body should contain a variety of food items. ( )
d) Meat alone. is sufficient to provide all nutrients to the body. ( )
b) (√)
c)(✓)
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Plastic is a polymer
-True
-False
TRUE
Explanation:
*not sure about this answer
Determine the effect each given mutation would have on the rate of glycolysis in muscle cells.
a. loss of binding site for fructose 1 ,6-bisphophate in pyruvate kinase.
b. loss of allosteric binding site for ATP in pyruvate kinase.
c. loss of allosteric binding site for AMP in phosphofructokinase.
d. loss of regulatory binding site for ATP in phosphofructokinase.
1. Increase
2. decrease
3. No effect
Answer:
a. Decrease
b. Increase
c. Increase
d. No effect
Explanation:
Glycolysis is present in muscle cells which converts glucose to pyruvate, water and NADH. It produces two molecules of ATP. Cellular respiration produces more molecules of ATP from pyruvate in mitochondria. Glycolysis increases in pyruvate kinase.
a. Loss of binding site for fructose 1,6-bisphosphate in pyruvate kinase: Decrease
b. Loss of allosteric binding site for ATP in pyruvate kinase: No effect
c. Loss of allosteric binding site for AMP in phosphofructokinase: Increase
d. Loss of regulatory binding site for ATP in phosphofructokinase: Increase
A. An important substrate in the glycolysis pathway is fructose 1,6-bisphosphate. It stimulates pyruvate kinase, an essential enzyme in glycolysis. The amount of pyruvate kinase that is activated will decrease if the fructose 1,6-bisphosphate binding site in pyruvate kinase is eliminated. As a result the rate of glycolysis in the muscle cells will probably decrease.
B. The allosteric ATP binding site of pyruvate kinase controls how active the enzyme is. However, pyruvate kinase is not significantly regulated by ATP in muscle cells. Therefore, it is unlikely that deletion of the ATP-binding allosteric site in pyruvate kinase would have no effect on the rate of glycolysis in muscle cells.
C. The rate-limiting enzyme in glycolysis, phosphofructokinase, is activated from all forms by AMP. It increases the rate of glycolysis by stimulating the activity of phosphofructokinase. If the allosteric binding site for AMP is eliminated, phosphofructokinase activation will be reduced. As a result, the rate of glycolysis in muscle cells will decrease.
D. Phosphofructokinase is inhibited allosterically by ATP. It regulates the rate of glycolysis by a feedback mechanism. High ATP concentrations cause phosphofructokinase to bind to its regulatory site, limiting its activity and delaying glycolysis. If the regulatory binding site for ATP is eliminated, the inhibitory action of ATP on phosphofructokinase would be lost. As a result, muscle cells will glycolysis at a faster rate.
Learn more about glycolysis, here:
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