Answer:
C. Molecular chaperones have been mutated.
Explanation:
In prokaryotes; transcription and translation occur consecutively. Protein doubling additionally happens following the translation. The heat stun proteins or molecular chaperones are imperative to assume a part in the appropriate collapsing of the protein. At high-ranging temperatures, the protein misfolding can be ascribed to a change in mutation of the molecular chaperones.
Yes because he is only observing the height of the plants and he only changes one variable
<span>Protein tertiary structures
are known to be a three dimensional structure of a protein with a single
polypeptide chain (backbone) and one or more protein secondary structures known as
protein domains.</span>
Tertiary Structure Interactions
1) Hydrophobic Interactions: they are non-
covalent bonds and very important in the formation of tertiary structure.
2) Ionic Bonds: the interaction of both positive
and negative amino acids forms a bond that helps to stabilize the protein molecules.
3) Hydrogen Bonds: this bond exit between the
amino acid with hydrophilic side chain found on the surface of the molecules and
water molecules in a solution.
4) Disulfide Bridges: it is a strong covalent bond commonly found between cysteine residues in close proximity space.
Answer:
While linebreeding is less likely to cause problems in the first generation than does inbreeding, over time, linebreeding can reduce the genetic diversity of a population and cause problems related to a too-small gene pool that may include an increased prevalence of genetic disorders and inbreeding depression
Explanation:
No it supports it by showing homologous structural traits
