How many places are there for electrons in the second shell of an atom? The answer is C) 8 electrons
Answer:
no
Explanation:
synthetic folic acid is way more harmful then the natural folate in foods, it may build up in the body and raise cancer, and synthetic copies of natural chemicals are not as good for you
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<u>A</u><u>nswer:</u></h2>
<u>Translation:</u> process of protein formation is called translation .
In the process of translation, a cell reads information from a molecule called a messenger RNA and uses this information to build a protein. Translation involves “decoding” a messenger RNA and using its information to build a polypeptide, or chain of amino acids
.
Translation involve three major steps
• Initiation ("beginning"): in this stage, the ribosome gets together with the mRNA and the first tRNA so translation can begin.
• Elongation ("middle"): in this stage, amino acids are brought to the ribosome by tRNAs and linked together to form a poly peptide chain.
•Termination ("end"): in the last stage of translation, the finished polypeptide is released to go and do its job in the cell.
<u>Organelles involve in translation:</u>
Ribosomes: main process of translation occour at ribosomes.
Rough endoplasmic reticulum: ribosomes are located on rough endoplasmicreticulum .it bound proteins in the vesicles.Vesicles containing proteins are budded off into cytoplasm and move toward golgi apparatus for further modification .
Golgi apparatus: synthesisezed proteins are not functional . In golgi apperatus they are further modefied and processed and stored for a short time and then released toward destination.
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!
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I believe the answer to this question is a food web.
Food Web definition: "<span>a series of organisms related by predator-prey and consumer-resource interactions; the entirety of interrelated food chains in an ecological community."
Source: </span>http://www.dictionary.com/browse/food-web
