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damaskus [11]
3 years ago
14

3A. A student slurry packed a silica gel column for the separation of 2-nitroanaline and 4-nitroanaline as described in the expe

riment given. During packing, they are not paying close enough attention and allow the top of the silica gel to run dry causing cracking within the silica gel. The student continues with the experiment and applies the mixture of isomers to the chromatography column. While the yellow band of the sample is being eluted, the student observes that there isn’t a clear separation with two separate yellow bands for each isomer and the band does not appear to be moving in a level band. Instead the band is slightly slanted What caused the poor separation of the isomers? What could the student do differently in the future to improve the results of the experiment?
Chemistry
1 answer:
Leto [7]3 years ago
5 0

Answer:

i like ya cut g

Explanation:

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Ira Lisetskai [31]
Three protons and three electrons. The protons are the plus signs because protons are positively charged, and the electrons are the minus signs because electrons are negatively charged. Also, the neutrons are the circles. Neutrons are negatively charged
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3 years ago
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. What mass of ammonium chloride must be added to 250. mL of water to give a solution with pH
Eduardwww [97]

The mass of ammonium chloride that must be added is : ( A ) 4.7 g

<u>Given data :</u>

Volume of water ( V )  = 250 mL = 0.25 L

pH of solution = 4.85

Kb = 1.8 * 10⁻⁵

Kw = 10⁻¹⁴

Given that the dissolution of NH₄Cl gives NH₄⁺⁺ and Cl⁻ ions the equation is written as :

NH₄CI  +  H₂O  ⇄  NH₃ + H₃O⁺

where conc of H₃O⁺

[ H₃O⁺ ] = \sqrt{Ka.C}   and Ka = Kw / Kb

∴ Ka = 5.56 * 10⁻¹⁰

Next step : Determine the concentration of H₃O⁺  in the solution

pH = - log [ H₃O⁺ ] = 4.85

∴ [ H₃O⁺ ] in the solution = 1.14125 * 10⁻⁵

Next step : Determine the concentration of NH₄CI in the solution

C = [ H₃O⁺ ]² / Ka

  = ( 1.14125 * 10⁻⁵ )² /  5.56 * 10⁻¹⁰

  = 0.359 mol / L

Determine the number of moles of NH₄CI in the solution

n = C . V

  = 0.359 mol / L  * 0.25 L =  0.08979 mole

Final step : determine the mass of ammonium chloride that must be added to 250 mL

mass = n * molar mass

         = 0.08979 * 53.5 g/mol

         = 4.80 g  ≈ 4.7 grams

Therefore we can conclude that the mass of ammonium chloride that must be added is 4.7 g

Learn more about ammonium chloride : brainly.com/question/13050932

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3 years ago
How does changing the temperature affect the chemical reaction?
tiny-mole [99]
The correct answer is C) Raising the temperature increases reaction rate by increasing the energy of the reacting atoms/ions/molecules and increases the number of collisions. 
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3 years ago
Phosphofructokinase is a four‑subunit protein with four active sites. Phosphofructokinase catalyzes step 3 of glycolysis, conver
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Answer:

1. PEP is a feedback inhibitor of phosphofructokinase.

4. PEP inhibition of phosphofructokinase yields a sigmoidal velocity versus substrate curve.

6. The binding of PEP to one phosphofructokinase subunit causes a conformation change that affects the ability of the substrate to bind to the other subunits.

Explanation:

Phosphofructokinase-1, PFK-1, is an allosteric enzymes composed of four protein subunits.

Allosteric enzymes are enzymes that function through non-covalent binding of allosteric modulators which may be activators or inhibitors. They produce a characteristic velocity versus substrate sigmoidal curve. PFK-1 has a separate binding site for its substrate, fructose-6-phosphate and it's allosteric modulators: ATP, ADP or phosphoenolpyruvate, PEP.

The enzyme can exist in two conformations, the T-state (tense) or the R-state (resting). Binding of substrate causes a conformational change from T-state to R-state, whereas binding of allosteric inhibitors returns it to the T-state.

PEP, the product of step 9 in glycolysis, is an allosteric inhibitor of PFK-1. When it binds to the the allosteric site, it leads to conformational changes in PFK-1 from the R-state to the T-state which reduces the enzymes ability to bind the substrate. These changes are responsible for the sigmoidal velocity/substrate curve in allosteric enzymes.

Therefore, the true statements from the options above are 1, 4, 6.

Options 2,3 and 5 are wrong because PEP is a negative effector of PFK-1, thus its binding reduces the affinity of PFK-1 for its substrate. Also, PFK-1 being an allosteric enzyme has separate binding sites for its substrate and its modulators. Thus, there is no competition for active site binding by substrate and modulators.

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Molarity times volume equals moles so 1 mole
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