Answer: D - Eukaryotic
Explanation: Can not be A, B or C
- Prokaryotic cells can not make up multicellular organisms
- Bacterial cells are prokaryotes and unicellular
- Not all multicellular organisms are plants and are therefore not all made of plant cells
When a cell is not dividing, the DNA is loosely spread throughout the nucleus in a threadlike form called chromatin.
Complete question:
You will find the complete question and answer in the attached files
Answer:
a) LL- <em> Long nose</em>
b) yy- <em>Blue body</em>
(c) Ss- <em>Squarepants body</em>
(d) RR- <em>Round eyes</em>
(e) Rr- <em>Round eyes</em>
(f) ll- <em>Stubby nose</em>
(g) ss- <em>Roundpants body</em>
(h) Yy- <em>Yellow body</em>
Explanation:
You will find the complete answer and explanation in the attached files due to technical problems.
Answer:
1250 g=1.25 Kg
Explanation:
We are given that Jason has five fishes of equally massed lead fish weights.
Weigh of each fish =250 grams
We have to find the value of total mass of the five lead fishing weights
Total number of fishes=5
In order to find the total mass we will use unitary method
Total mass is obtained by multiplying the total number of fishes with weight of one fish
Total mass=
Total mass of five fishes=1250 g
1 kg =1000g
Then 1250 g=
Hence, total mass of five lead fishing weights=1250 g=1.25 Kg
Answer:
One of the common genetic disorders is sickle cell anemia, in which 2 recessive alleles must meet to allow for destruction and alteration in the morphology of red blood cells. This usually leads to loss of proper binding of oxygen to hemoglobin and curved, sickle-shaped erythrocytes. The mutation causing this disease occurs in the 6th codon of the HBB gene encoding the hemoglobin subunit β (β-globin), a protein, serving as an integral part of the adult hemoglobin A (HbA), which is a heterotetramer of 2 α chains and 2 β chains that is responsible for binding to the oxygen in the blood. This mutation changes a charged glutamic acid to a hydrophobic valine residue and disrupts the tertiary structure and stability of the hemoglobin molecule. Since in the field of protein intrinsic disorder, charged and polar residues are typically considered as disorder promoting, in opposite to the order-promoting non-polar hydrophobic residues, in this study we attempted to answer a question if intrinsic disorder might have a role in the pathogenesis of sickle cell anemia. To this end, several disorder predictors were utilized to evaluate the presence of intrinsically disordered regions in all subunits of human hemoglobin: α, β, δ, ε, ζ, γ1, and γ2. Then, structural analysis was completed by using the SWISS-MODEL Repository to visualize the outputs of the disorder predictors. Finally, Uniprot STRING and D2P2 were used to determine biochemical interactome and protein partners for each hemoglobin subunit along with analyzing their posttranslational modifications. All these properties were used to determine any differences between the 6 different types of subunits of hemoglobin and to correlate the mutation leading to sickle cell anemia with intrinsic disorder propensity.
Explanation:
