Answer:
The correct answer is "Redwood tree; human being; Paramecium; White Blood Cell; Escherichia coli; Chickenpox virus; Ribosome; Prion fibril; Water molecule; Sulfur atom".
Explanation:
Redwood trees are gigantic trees, and its size can reach up to 90 meters.
The average size of a human being is 1.7 meters for males and 1.6 meters for females.
Paramecium are members of the protozoa genus, among the largest unicellular algae. Its average size is among 50 to 330 micrometers.
White Blood Cell are up to 17 micrometers in diameter.
Escherichia coli is a type of bacteria, as a prokaryotic organism is much more smaller than a eukaryotic cell such asa the white blood cell. Escherichia coli is up to 2 micrometers in diameter.
Chickenpox virus are among the largest viruses, they are from 150 to 200 nanometers in diameter.
Ribosomes vary on size depending if they are Prokaryotic or Eukaryotic, where the first are up to 20 nanometers and the second are up to 30 nanometers.
Prion fibrils are aggregates comprised of several protein units. It size varies depending on the number of proteins, but the ones containing around 200 units can reach up to 27 nanometers.
Water molecule is comprised of two atoms of oxygen and one atom of hydrogen, its size is measured with picometers (1 picometer is equal to 1000 nanometers). A water molecule has a size of 275 picometers.
Sulfur atom is the smallest in the list. Its size is around 100 picometers.
Hydrogen, Carbon, Nitrogen, and Oxygen all make up amino acids.
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:
<span>Tsetse flies feed by piercing the skin with their mouthparts and: Sucking the blood of animals and humans. </span>
