The National Institutes of Health found it effective in reducing pain and other symptoms, but it is not clear how it works.
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:
Pepsin digests potato because it mainly contains starch
The molecule that is least likely to be a subunit of a macromolecule is the steroids.
<h3>What are macromolecules?</h3>
The term macromolecules refers to those molecules that are large and are composed of smaller subunits that are joined together to form the macromolecule. These subunits are called the monomers of the macromolecule that is under study.
We know that the steroids are already large molecules in themselves thus they can not be joined together to form a bigger molecule.
Hence, the molecule that is least likely to be a subunit of a macromolecule is the steroids.
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Missing parts:
Subunits sometimes build up to form a macromolecule. which molecule is least likely to be comprised of subunits? A. glucose. B. amino acids. C. steroids
THE EFFECT IS TREYWAY 6IX9INE
