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Kamila [148]
3 years ago
10

Black fur is dominant to brown hair in guinea pigs. Incomplete dominance is exhibited in guinea pigs with gray and white hair. W

hat could you do to determine the genotype of guinea pig with black fur?
Mate the black guinea pig with a brown guinea pig.

Mate the black guinea pig with another black guinea pig.

Mate the black guinea pig with a white guinea pig.

Mate the black guinea pig with a gray guinea pig.
Biology
2 answers:
astra-53 [7]3 years ago
5 0

Answer:

Mate the black guinea pig with a brown guinea pig.

Explanation:

Mating must be done with a brown guinea pig, since this type of mating will enable to determine the presence of heterocigotes "black hair" by calculating the frequency in the progeny

dmitriy555 [2]3 years ago
3 0

Answer:

B

Explanation:

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The correct answer Is true
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Pls help (WILL GIVE BRAINLIEST)\ AND A BUNCH OF POINTS
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Answer:

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Explanation:

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2 years ago
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OlgaM077 [116]

Answer:

Option D = 3.4 g/mL

Explanation:

Given data:

Volume of water = 21.2 mL

Volume of water + object = 27.8 mL

Mass of object = 22.4 g

Density of object = ?

Solution:

First of all we will calculate the volume of object.

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Density of object:

d = m/v

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4 0
3 years ago
Name the four levels of structure of proteins and explain what each level is responsible for adding to the protein structure.
erik [133]
Tertiary Structure<span> - refers to the comprehensive 3-D structure of the polypeptide chain of a </span>protein<span>. There are several types of bonds and forces that hold a protein in its tertiary structure. </span>Hydrophobic interactions<span> greatly contribute to the folding and shaping of a protein. The "R" group of the amino acid is either hydrophobic or hydrophilic. The amino acids with hydrophilic "R" groups will seek contact with their aqueous environment, while amino acids with hydrophobic "R" groups will seek to avoid water and position themselves towards the center of the protein. </span>Hydrogen bonding<span> in the polypeptide chain and between amino acid "R" groups helps to stabilize protein structure by holding the protein in the shape established by the hydrophobic interactions. Due to protein folding, </span>ionic bonding<span> can occur between the positively and negatively charged "R" groups that come in close contact with one another. Folding can also result in covalent bonding between the "R" groups of cysteine amino acids. This type of bonding forms what is called a </span>disulfide bridge<span>. </span>Primary Structure - describes the unique order in which amino acids are linked together to form a protein. Proteins are constructed from a set of 20 amino acids. <span>All amino acids have the alpha carbon bonded to a hydrogen atom, carboxyl group, and amino group. The </span>"R" group<span> varies among </span>amino acids<span> and determines the differences between these protein monomers. The amino acid sequence of a protein is determined by the information found in the cellular</span>genetic code<span>. The order of amino acids in a polypeptide chain is unique and specific to a particular protein. Altering a single amino acid causes a </span>gene mutation, which most often results in a non-functioning protein.
<span>Secondary Structure - refers to the coiling or folding of a polypeptide chain that gives the protein its 3-D shape. There are two types of secondary structures observed in proteins. One type is the alpha (α) helix structure. This structure resembles a coiled spring and is secured by hydrogen bonding in the polypeptide chain. The second type of secondary structure in proteins is the beta (β) pleated sheet. This structure appears to be folded or pleated and is held together by hydrogen bonding between polypeptide units of the folded chain that lie adjacent to one another.
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3 0
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Monica [59]
I would say the growth, the repair, and the reproduction.
6 0
3 years ago
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