C, because it doesn't matter if they all have the same genders but the functions of the body with the other options could affect the babies body.
A list of the cell fibers from largest to smallest would read:
1. microtubules – is a microscopic tubular structure that is present in numbers in the cytoplasm of cells. These are usually aggregated to form complex structures.
<span>2. intermediate filaments – are cytoskeletal components that is usually found in the cells of vertebrate species and </span>other organisms like plants, fungi, unicellular organisms.
3. <span>Microfilaments – are filamentous structures that can be found in the cytoplasm of eukaryotic cells and it will form part of the </span>cytoskeletons<span>. They are composed primarily of polymers of actin. But in cells, they usually interact with other proteins.</span>
Alcoholic fermentation; carbon dioxide. Alcoholic fermentation produces alcohol and carbon dioxide in bread. The alcohol evaporates during the baking process.
Heat creates energy... the atoms move faster and faster, which changes the state of matter.
for example:
if a solid is heated, it turns to a liquid
if a liquid is heated, it turns to a gas
hope this helps?
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>
