Hi there!
<u>Electronegativity</u> is the concept of how likely an atom is to attract the shared molecules in one of these bonds to itself. We know the molecule water is made up of two hydrogens and one oxygen. The electronegativity of hydrogen is 2.2, and oxygen 3.4. An <u>ionic bond</u> needs at least a difference in electronegativity of 1.6. As the difference is less than that, we can say that water is a covalent molecule. This then wipes out choice B, because it is not ionic, and C, as we have seen it is actually covalent.
Now, we can see the difference in electronegativity between oxygen and hydrogen is still 1.2. This means that while it is not at the point for there to be an ionic bond, there is still a difference in attraction, where the electrons will tend to favor the oxygen more and 'hang around it' more. As electrons are <u>negatively charged</u><em><u>,</u></em> this means that the oxygen will gain a slightly negative charge. This then makes the molecule polar, because it now has a charge within the molecule. This means we have our answer, choice D.
In terms of hydrophobic molecules - they tend to be ones without a charge. (If you're interested in this kind of stuff, I'd search hydrophobic up, and possibly also look into hydrogen bonds).
Hope this helps! Feel free to ask me any other questions you have about this specific problem.
Answer:
Function and structure are related, because of a certain structure a living thing make contain makes the object function the way it does.
The relationship of a structure and function is the structuring levels from molecules to organism ensure successful functioning in all living organism and living system.
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:
active transport <span>Which transport process requires atp utilization</span>
