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shtirl [24]
3 years ago
10

Element Y has two natural isotopes Y-63 (62.940 amu) and Y-65 (64.928 amu). Calculate the atomic mass of element Y, given the ab

undance of Y-63 is 69.17%?
Chemistry
1 answer:
djverab [1.8K]3 years ago
5 0

Answer:

Average atomic mass = 63.553 amu.

Explanation:

Given data:

Abundance of Y-63 = 69.17%

Abundance of Y-65 = 100 - 69.17 = 30.83%

Atomic mass of Y-63 = 62.940 amu

Atomic mass of Y-65 = 64.928 amu

Atomic mass of Y = ?

Solution:

Average atomic mass= (abundance of 1st isotope × its atomic mass) +(abundance of 2nd isotope × its atomic mass)  / 100

Average atomic mass= (62.940×69.17)+(64.928×30.83) /100

Average atomic mass =  4353.560 + 2001.730 / 100

Average atomic mass = 6355.29 / 100

Average atomic mass = 63.553 amu.

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Answer:

V₂ = 0.4 L

Explanation:

<u>Data:</u>

  • P₁ (initial pressure) = 500 torr
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<u>Wanted:</u>

  • V₂ (final volume)

<u>Equation:</u>

  • P₁V₁ = P₂V₂  →  V₂ = P₁V₁ / P₂

<u>Solution:</u>

  • V₂ = \frac{(500 torr)(0.5 L)}{700 torr} = 0.3571 L or 0.4 L
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An experimental spacecraft consumes a special fuel at a rate of 372 L/min. The density of the fuel is 0.730 g/mL and the standar
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Explanation:

First, we will calculate fuel consumption is as follows.

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Now, we will calculate the power as follows.

        Power = Fuel consumption rate × -enthalpy of combustion

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3 years ago
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Answer:

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5 0
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The lock-and-key model and the induced-fit model are two models of enzyme action explaining both the specificity and the catalyt
ivolga24 [154]

Answer:

The lock-and-key model:

c. Enzyme active site has a rigid structure complementary

The induced-fit model:

a. Enzyme conformation changes when it binds the substrate so the active site fits the substrate.

Common to both The lock-and-key model and The induced-fit model:

b. Substrate binds to the enzyme at the active site, forming an enzyme-substrate complex.

d. Substrate binds to the enzyme through non-covalent interactions

Explanation:

Generally, the catalytic power of enzymes are due to transient covalent bonds formed between an enzyme's catalytic functional group and a substrate as well as non-covalent interactions between substrate and enzyme which lowers the activation energy of the reaction. This applies to both the lock-and-key model as well as induced-fit mode of enzyme catalysis.

The lock and key model of enzyme catalysis and specificity proposes that enzymes are structurally complementary to their substrates such that they fit like a lock and key. This complementary nature of the enzyme and its substrates ensures that only a substrate that is complementary to the enzyme's active site can bind to it for catalysis to proceed. this is known as the specificity of an enzyme to a particular substrate.

The induced-fit mode proposes that binding of substrate to the active site of an enzyme induces conformational changes in the enzyme which better positions various functional groups on the enzyme into the proper position to catalyse the reaction.

4 0
2 years ago
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