Non-random mating is assortative mating. It is a pattern and form of sexual selection in which individuals with similar phenotypes mate with one another more frequently than would be expected under a random mating pattern. non-random mating can act as an ancillary process for natural selection to cause evolution to occur. It’s also bad for evolution because any departure from random mating upsets the equilibrium distribution of genotypes in a population. Recombination is a process by which pieces of DNA are broken and recombined to produce new combinations of alleles. recombination is important to somatic cells in eukaryotes because it can be used to help repair broken DNA. recombination by itself does not cause evolution to occur. Rather, it is a contributing mechanism that works with natural selection by creating combinations of genes that nature selects for or against. Non-random mating affects the evolution more than recombination
Betta fish are also known as Siamese fighting fish.They flare their gills when they are ready to fight. This makes them appear larger since fish do not have very good eyesight. They also fan their gills when they are trying to court a female Betta. ... Bettas are one of the few fish that can get air from above the water.
It is water pollution, since you are polluting the river.
Hope I helped!
Cytochalasin D prevents the addition of monomers at plus ends of existing filaments. When the concentration of G-actin in the cytosol is below the critical concentration, the loss of monomers at <span>minus ends</span> of existing filaments eventually results in their shortening. This occurs despite the pool of available G-actin in the cytosol.
Answer:
The correct answer is - altered primary and quaternary structure; secondary and tertiary structure may or may not be altered.
Explanation:
a) Primary structure: It is fundamentally the amino acid sequence or arrangments. Every protein has a remarkable amino acid sequence and little change in these sequence modifies the primary structure. On account of sickle cell, the amino corrosive has changed, and henceforth the essential structure of the protein molecule changes.
b). secondary structure: It is the folding of the primary structure chain, which results from intermolecular and intramolecular hydrogen holding of the amide group. Ex; Alpha helix and beta sheets. In the above case, this may or might not have changed as there is no conclusive method to know this.
c) Tertiary structure: Most proteins' tertiary structures are mixes of a-helices, b sheets, and circles and turns. Every protein has interesting three-dimensional structure, folded in a particular way now and then known as a domain. For our situation, since it depends on the optional structure, it might have changed.
d) Quaternary structure: It is the relationship of numerous individual protein chains into a solitary protein with various subunits. The subunits arrangment offers to ascend to a steady structure. For our situation, a hemoglobin tetramers partner with one another and gather into large fibers. This has changed the first structure and accordingly we state the quaternary structure has changed.
