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My name is Ann [436]
2 years ago
12

The diagram represents a dihybrid cross between two pea plants heterozygous for both seed color and seed shape. mc021-1.jpg What

is the phenotypic ratio of the offspring? 1:1:1:1:2:2:2:2:4 1:3:3:9 1:4 4:12

Biology
2 answers:
suter [353]2 years ago
7 0

Answer:

B. 1:3:3:9

Explanation:

bija089 [108]2 years ago
5 0
The correct answer is 9:3:3:1

When two homozygotes for two traits cross, the phenotypic ratio of the offspring is 9:3:3:1 ( unless other factors like epistatic interaction change the inheritance model).
In our case, we have two simple traits of seed color and seed shape that follow the Mendelian model of inheritance.

In this dihybrid cross, we have
9/16 of the offspring expressing both dominant traits ( yellow and round seeds)
3/16 expressing one dominant and one recessive trait ( yellow and wrinkled)
3/16 expressing the other dominant and recessive trait (green and round)
1/16 expressing both recessive traits ( green and wrinkled)

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Explanation:

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Some anthropogenic sources of groundwater pollution are

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Groundwater holds its contamination and pollutants that cause pollution whereas surface water rinses their contamination and pollutants.

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The answers are as follows:
1. <span>An inhibitor has a structure that is so similar to the substrate that it can bond to the enzyme just like the substrate: t</span>his is called competitive inhibitor. A competitive inhibitor will compete with the substrate for the active site of the enzyme and bind to the active site, thus incapacitating the substrate from binding to the active site.
2.  An inhibitor binds to a site on the enzyme that is not the active site: this is called non competitive inhibitors. Non competitive inhibitors bind to other site in the enzyme which is not the active site of the enzyme. The binding of the inhibitor changes the conformation of the enzyme as well as the active site, thus making it impossible for the substrate to bind to the enzyme effectively.
3. <span>usually, a(n) inhibitor forms a covalent bond with an amino acid side group within the active site, which prevents the substrate from entering the active site or prevents catalytic activity: this is called irreversible or permanent inhibition. Permanent inhibitors form covalent bonds with the enzyme and prevent substrate from binding to the enzyme.
4. T</span><span>he competitive inhibitor competes with the substrate for the ACTIVE SITE on the enzyme: The active site of an enzyme is the place where the substrate normally bind in order to activate a enzyme. Competitive inhibitors are those inhibitors that compete with the substrate for the active site of the enzyme and prevent the substrate from binding there.
5. W</span><span>hen the noncompetitive inhibitor is bonded to the enzyme, the shape of the ENZYME is distorted. The non competitive inhibitors are those inhibitors that bind to other places in the enzyme instead of the active site. The binding of the non competitive inhibitor usually distort the shape and the conformation of the enzyme thus preventing the substrate from binding to it effectively.
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