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Answer:
- time: 1.122 seconds
- range: 10.693 m
- maximum height: 1.543 m
Explanation:
<u>Given</u>:
runner is launched at 30° angle to horizontal at 11 m/s
acceleration due to gravity is g = -9.8 m/s²
<u>Find</u>:
runner's hang time
runner's distance to the landing point
runner's maximum height
<u>Solution</u>:
The (horizontal, vertical) speed components will be ...
(11 m/s)(cos(30°), sin(30°)) = (5.5√3 m/s, 5.5 m/s)
The time of flight can be found from the height formula:
h(t) = 1/2gt² +vt . . . . . . where v is the vertical speed at launch
The time we're concerned with is the time when h(t)=0 and t>0.
0 = -4.9t^2 +5.5√3t = t(-4.9t +5.5√3)
The second factor is zero when ...
t = (5.5√3)/4.9 ≈ 1.122 . . . seconds hang time
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The distance to the landing point will be the product of horizontal speed and hang time:
d = (5.5 m/s)(5.5√3/4.9 s) ≈ 10.693 m . . . . distance to landing
__
The maximum height can be found from the formula (based on conversion of kinetic energy to potential energy) ...
h = v²/|2g| = (5.5 m/s)²/(2(9.8 m/s²)) ≈ 1.543 m . . . . maximum height
The pituitary gland is known as the "master gland" because it is known to control hormones that regulate several other important systems in the endocrine system such as the thyroid gland, ovaries, and testes.
It acts like its nothing there .
It must be durable and available
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:
