Answer:
B. The allele frequency of T is 0.84, and the allele frequency of t is 0.16.
Explanation:
The Hardy-Weinberg equation is:
p2 + 2pq + q2 = 1
Where:
p = the frequency of the dominant allele
q = the frequency of the recessive allele
1 = the total number of alleles
Given that 16 individuals out of 100 are unable to taste PTC, we can calculate that the frequency of the recessive allele, q, is 0.16. We can then use the Hardy-Weinberg equation to solve for the frequency of the dominant allele, p:
p2 + 2pq + q2 = 1
p2 + 2p(0.16) + (0.16)2 = 1
p2 + 0.32p + 0.0256 = 1
p2 + 0.32p - 0.9144 = 0
(p + 0.32)(p - 2.84) = 0
p = -0.32 or p = 2.84
Since the allele frequencies must add up to 1, we know that p cannot equal -0.32. This leaves us with p = 2.84. Therefore, the allele frequency of the dominant allele is 2.84, and the allele frequency of the recessive allele is 0.16.
It helps it because it is designed in a way that causes the molecular science of the system to equal the same length as the area of the radius. hope I helped?!
Answer:
About 20 percent of all oxygen produced comes from the Amazon.
Answer:
Option A, hydrophilic/hydrophobic forces
Explanation:
The cytoplasmic membrane consists of phospholipids which have both the hydrophilic and hydrophobic regions and hence are amphipathic in nature. Due to this structural complexity, phospholipids produces barrier both at the interior and exterior of cell and hence form a membrane bilayer under suitable conditions. For instance when it is in water, it arrange itself in a way that their hydrophobic tails lie at the inner side and hydrophilic heads face outer side.
Hence, option A is correct
Answer:
thermodynamically unstable but kinetically stable.
Explanation:
The complete question is as follows:
Under physiological conditions, peptide bond formation and degradation both require enzymes, but only formation requires coupling to GTP hydrolysis. Based on this information, peptide bonds under physiological conditions are:
A. both thermodynamically and kinetically stable.
B.thermodynamically unstable but kinetically stable.
C.thermodynamically stable but kinetically unstable.
D. both thermodynamically and kinetically unstable.
- The term thermodynamically unstable refers to the fact that the peptide bonds are prone to breakage under physiological conditions.
- The reason why one can conclude the thermodynamic instability of the peptide bonds under physiological condition is that there is a need for a source of energy i.e. GTP hydrolysis for the formation of the peptide bond.
- The fact that the breakage of peptide does not require any input of energy but the only formation does confirms the fact that under physiological conditions they are thermodynamically unstable.
- Even though they are thermodynamically unstable, they are kinetically stable because both the formation and degradation require enzymes.
- The function of enzymes is to decrease the activation energy and hence, increase the rate of reaction. This means that if the enzymes are absent the rate of breakage of peptide bonds would be really slow this points out to the fact that they are kinetically stable under physiological conditions.
