Answer:
Elements that are found in the same horizontal row (belong to the same period) in the periodic table, e.g. Fluorine and Neon both have the same energy level of 2.
<em>Note: The question does not specify any two elements.</em>
Explanation:
The modern periodic table is organized into eight vertical columns known as groups and seven horizontal rows known as periods. The atomic number ( number of protons in the nucleus) of elements increases when moving across the periodic table from left to right. The horizontal rows or periods represents an energy levels or the number of electron shells in an element. Energy levels (also called electron shells) are fixed distances from the nucleus of an atom where electrons may be found. Elements belonging to the same period have the same number of energy level or shells. For example, the elements belonging to Period 2 include lithium, beryllium, boron, carbon, nitrogen, oxygen, fluorine and neon. These all have the same number of energy level of 2.
Hereditary is Breast cancer and Inheritance is
Getting Breast Cancer basically it runs in the family inheriting.
It becomes more alkaline where pH will be more than 8
Incomplete dominance shows phenotypes of both dominat and reccessive trait !!
so supppose red is AA
the white is aa
and pink is Aa (heterozygous thus pink)
on crossing Aa to Aa (two pink)
we have ; AA , Aa, Aa, aa
thus 1 red, 2 pink, 1 white
Ratio - 1:2:1
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:
