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sveticcg [70]
3 years ago
9

Which characteristic of life relies on the sun

Biology
2 answers:
Liono4ka [1.6K]3 years ago
8 0
The answer should be solar power .
lyudmila [28]3 years ago
4 0
All characteristics of life rely on the sun.
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Describe the forms that water takes through out the water cycle
Aleks [24]

Gas: when the water has evaporated and is now out in the air. Water molecules move super fast during this stage.

Liquid: Water molecules have a good amount of space to move around, but they aren’t traveling as fast as they do in the gastric state.

Solid: ice in other words, the water molecules are super tight and compact, but are still moving around, just not very fast.

4 0
3 years ago
Explain two theories of color vision in humans. How does one of them explain color deficiency?
Alborosie
<span>There are two major theories that will explain on research on colour vision. They are 1. the trichromatic theory also known as the Young-Helmholtz theory 2. opponent-process theory. These two theories explain processes that operate at different levels of the visual system.</span>
3 0
3 years ago
How do I know the phenotype and genotype percentage on a punnet square?
Nesterboy [21]

Answer:

Phenotypes are physical attributes. Genotypes are the alleles.

The phenotypes are 75% green peas and 25% yellow peas. This is because the capital G is a dominant allele and green is the dominant attribute and as long as 1 G is present, then the pea will appear green.

The genotypes are 25% GG, 50% Gg, and 25% gg.

Please thank!

3 0
3 years ago
When looking at sea breezes and land breezes, water has higher specific heat than the land so it…
jok3333 [9.3K]

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c. warms slowly, but holds heat longer

5 0
2 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.
</span><span>Quaternary Structure - refers to the structure of a protein macromolecule formed by interactions between multiple polypeptide chains. Each polypeptide chain is referred to as a subunit. Proteins with quaternary structure may consist of more than one of the same type of protein subunit. They may also be composed of different subunits. Hemoglobin is an example of a protein with quaternary structure. Hemoglobin, found in the blood, is an iron-containing protein that binds oxygen molecules. It contains four subunits: two alpha subunits and two beta subunits.

I hope this helped you find the answer you were looking for!

</span>
3 0
2 years ago
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