As you talk in animals
nucleus/ plasma membrane / mitochondria
if you talk in plants
nucleus / the cell / plastid / mitochondria
Leucine (Leu) and essential amino acid (Ile) are unit isomers of each other with terribly similar structures and properties. They each have Hydrophobic facet chains of an analogous size. As each residues area unit H'phobic, they're going to attempt to bury themselves within the interior of the macro-molecule to minimize disruption to the water H-bonding network, driven by the Hydrophobic interaction. thus in wild kind and mutant protein, each Leu and Ile are going to be in very similar position. Because of them being isomers, they need similar facet chain geometries thus there will not be any issue with steric constraints, in order that they can each occupy a awfully similar area within the hydrophobic core of the macro-molecule.
As within the wild sort catalyst, Leu is within the situation, it's possibly concerned within the mechanism of the catalyst. but a Leu mutation can conserve the properties of the residue that are necessary for chemical action. they're fairly nonreactive facet chains, thus are possibly concerned in binding of the substrate through the H'phobic interaction. thus the mutation might slightly decrease the affinity of the catalyst for the substrate, and reduce the speed of chemical action somewhat.
The answers;
1. Termination. Out of the 64 codons, UAG, UAA, and UGA are the stop codons that terminate translation when encountered by the ribosome. These three do not code for any amino acid but rather cause the translation complex to dislocate.
2. Translation. In this process, the ribosome ‘reads’ the codon and brings in a t-RNA with an anticodon to the codon. This tRNA carries a specific amino acid (for that codon) and engages in the P-site of the ribosome. The amino acid is taken from the t-RNA and used to elongate the polypeptide chain being formed. Thereafter the empty t-RNA dislocates.
3. Aminoacyl-tRNA synthetase. When a tRNA brings in an amino acid to the initiation complex, it is dislocated when ‘empty’. Aminoacyl-tRNA synthetase then catalyzes the reattachment of another amino acid through a chemical reaction called esterification. The cognate tRNA then become an aminoacyl-tRNA.
4. tRNA . Every tRNA has an amino acid attached to it. The type of amino acid (out of the 22 amino acids) is determined by the anticodon on the tRNA. There are many codons that are amino acids meaning that there are redundant codons that specify for the same amino acid.
5. Initiation. Initiation begins by the formation of an initiation complex. This complex is comprosed by the two subunits of the ribosome, and the mRNA. The complex becomes compelete when a Met-tRNA (a tRNA with a methionine amino acid) engages the P-site and then translation begins.
Answer:
Organisms show a steady increase in diversity, interrupted by extinction events.
Explanation:
Limiting factors are factors that can change growth rate of the populations. Limiting factors are the availability of food, water, shelter, disease or relationships between organisms like competition for resources or predation. So, for example, if one animal's population decreases (due to disease), the population of animals that eats that animal might also decrease (due to decreased food).
Infectious agents might be transmitted through the direct contact (person-to person or droplet spread) or indirectly through the airborne transmission, contaminated objects, insect bites, water and food, animal-to-person contact..