Answer:
The correct option is B.<u> It was mostly incorporated into proteins that regulate and manage metabolic reactions.</u>
Explanation:
The results of the experiment showed that most of the radiolabeled amino acids were present in the mitochondria.
Amino acids can be described as organic compounds which build up the proteins. There are 20 different kinds of amino acids which make up different kinds of proteins, each specified to perform specific functions.
The results from the experiment prove that the radiolabeled amino acid is being used to make proteins that are necessary for metabolic reactions.
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.
6. E</span><span>nzyme inhibitors disrupt normal interactions between an enzyme and its SUBSTRATE. The principal function of enzyme inhibitor is to prevent the substrate from binding to the appropriate enzyme. This is usually done in the human system in order to regulate the activities of enzymes.</span>
Answer:
a)by providing water for irrigation and restoring trees to areas where forests once existed
Explanation:
:)
<span>Expanding red giant stars will swallow too-close planets. In the solar system, the sun will engulf Mercury and Venus, and may devour Earth, as well. So logically concluding, the answer must be that it would devour the planets whole, and there will be no rotation, (assuming this is a trick question)</span>
This is the DNA. I'm going to only use the upper strand to demonstrate what this strand would code for before and after a single bp deletion (so write it as mRNA). I will also write it how it's easier to see this which is to split them up into the 3 base codon system. Note that you don't need to know the amino acid code - you use a table to find these.
ORIGINAL (mRNA on top, Amino Acid (AA) on bottom:
5'-AGC GGG AUG AGC GCA UGU GGC GCA UAA CUG-3'
SER GLY MET SER ALA CYS GLY ALA STOP LEU
Note that the protein would stop being made at the stop codon and the LEU wouldn't matter at the end...
Now, I will remove one bp...(I bolded it up top). Rewrite the mRNA and find the corresponding AA...
NEW
5'-AGC GGG AUG GCG CAU GTG GCG CAU AAC UG-3'
SER GLY MET ALA HIS VAL ALA HIS ASN .....
Completely different amino acid sequence after the methionine (MET). The stop codon is gone...the protein would continue being translated until it reaches another stop codon...so not what was supposed to be made!
