Domain (Specifically domain Eukarya)
Answer:
Explanation:
<em>The probability of producing plants with white axial flowers would be 1/16.</em>
From the illustration, All F1 individuals had red, axial flowers. It thus means that red and axial genes are dominant over white and terminal genes in the pea plant.
Let us assume that the allele for flower color is A (red) and a (white); and the allele for flower location is B (axial) and b (terminal).
Pure-breeding red, axial flower = AABB
Pure breeding white, terminal flower = aabb
AABB x aabb
F1 genotype = AaBb - all red and axial
At F2:
AaBb x AaBb
Progeny
<em>9 A_B_ red/axial</em>
<em>3 A_bb red/terminal</em>
<em>3 aaB_ white/axial</em>
<em>1 aabb - white/terminal</em>
Hence, the probability of producing plants with white axial flowers in the F2 generation is 1/16.
Answer:
Longest interval during which no tree-cutting sample occurred: 9 years (1203 AD - 1212 AD)
First year in that interval: 1203 AD
Explanation:
Lets complete the question first.
Q) A study uses tree rings to determine the year in which a tree was cut. The data is shown in the leaf and stem diagram in the ATTACHMENT.
The three digits number in the left column represents centuries and decades AD. The numbers on the right represents the years.
For example, consider the first input in the diagram
119 | 5 6
which means it represents 2 samples.
1195 AD, 1196 AD.
The longest interval with no tree-cutting samples is found from 1203 AD to 1212 AD.
The correct option is ANALOGOUS STRUCTURES.
Analogous structures are structures that are similar because of the functions they carry out and because of their external appearance. But these structures are different internally.<span />
Answer:
Molecular chaperons in the cells helps in protein folding. These are the group of proteins that have functional similarity and they also assist protein folding.
They have the ability to prevent the non specific binding and aggregation by the binding of the non native proteins.
Molecular chaperons helps in recognizing the hydrophobic surfaces of the unfolded proteins because they themselves are hydrophobic in nature and will combine to the hydrophic binding and bonding.
This helps in guiding the protein to folding.
