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erastovalidia [21]
3 years ago
7

The presence of a negative allosteric effector on an allosteric protein would: a. cause a shift to the left in the sigmoidal cur

ve. b. increase the number of R conformations. c. decrease the cooperativity of the substrate. d. raise the apparent value of the equilibrium constant, L. e. increase the likelihood of the binding of S.
Biology
1 answer:
Feliz [49]3 years ago
4 0

Answer:

d. raise the apparent value of the equilibrium constant, L.

Explanation:

Allosteric regulation is a type of regulation of an enzyme by binding an effector molecule at a site other than the protein's active site (i.e., the allosteric site). The equilibrium constant (L) refers to the transition between two forms of an allosteric protein in absence of a ligand. The properties of allosteric enzymes are explained by conformational changes associated with a low-affinity tense (T) state, or a high-affinity relaxed (R) state. Negative allosteric effectors are molecules that bind to the allosteric site on an enzyme in order to decrease its activity, thereby leading the enzyme to a low activity T state and thus increasing the value of the equilibrium constant.

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1) CO₂

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Explanation:

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1) The gas produced is CO₂.

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Convert to moles:

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Find moles of CaCO₃:

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Convert to mass:

(0.002213 mol CO₂) (44.01 g / mol) = 0.09738 g CO₂

Calculate mass of MgCO₃:

(0.5236 g) (0.5770) = 0.3021 g MgCO₃

Convert to moles:

(0.3021 g MgCO₃) (1 mol / 84.31 g) = 0.003583 mol MgCO₃

Find moles of MgCO₃:

(0.003583 mol MgCO₃) (1 mol CO₂ / mol MgCO₃) = 0.003583 mol CO₂

Convert to mass:

(0.003583 mol CO₂) (44.01 g / mol) = 0.1577 g CO₂

Total mass of CO₂:

0.09738 g CO₂ + 0.1577 g CO₂ = 0.2551 g CO₂

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