Answer:
1. The difference between the normal hemoglobin protein DNA sequence and the sickle cell hemoglobin DNA sequence is a base to base shift, in this case adenine (GAG) to thymine (GTG).
2. The difference affects the amino acid sequence of the protein by replacing glutamic acid (Glu) with valine (Val).
Explanation:
In sickle cell anemia, a change in the DNA nucleotide sequence is observed, where adenine is substituted by thymine, whose expression is the change in the amino acid sequence of globine β, incorporating valine instead of glutamic acid. This represents a molecular mutation - point mutation - by subtitution, which corresponds to missense mutation.
<u>Normal hemoglobin protein in a RBC</u>
DNA CTG ACT CCT GAG GAG AAG TCT
Amino acids Leu Thr Pro Glu Glu Lys Ser
<u>Sickle cell hemoglobin protein in a RBC</u>
DNA CTG ACT CCT <em>GTG</em> GAG AAG TCT
Amino acids Leu Thr Pro <em>Val</em> Glu Lys Ser
When GAG is transcribed to mRNA, the CUC codon is obtained, which codes for glutamic acid. Thymine substitution causes the DNA sequence to change to GTG, which is transcribed as CAC, the codon that encodes the amino acid valine. The <u>change from glutamic acid to valine in β-globin causes an altered hemoglobin, giving the abnormal erythrocytes observed in sickle cell disease</u>.
1. Swimming
2. Diving
3. Respiration
4. Salt secretion
5. Sea turtles on land
I think these are the answers.
Answer:
The intracellular is where enzymes need to perform optimally or near optimum.
Explanation:
The Km is the concentration of molecules where an enzyme performs at half of its maximum velocity (Vmax). Therefore, when molecules are near Km the enzyme is able to hydrolyze molecules nearer its Vmax.
Answer:
Petiole
Explanation:
The petiole is the part of the leaf that attaches the leaf to the main stem of the plant. Depending on the leaf structure of the plant, some leaves may be devoid of a petiole, and be regarded as apetiolate.
Answer:
b) In allosteric regulation, a small molecule binds to a large protein and causes it to change its shape and activity.
Explanation:
Allosteric regulation refers to the activity control of an enzyme by binding small molecules to regulatory sites on It. This binding causes an alteration of the protein conformation and consequently the shape of the active site and its catalytic activity are altered. Regulatory enzymes can act by either stimulating or inhibiting the activity of a protein.
