Answer:
The protein likely travels through a common lumen shared by thylakoid membranes and grana, and cannot easily diffuse through the thylakoid membrane.
Explanation:
There is a lot of scientific research in which a specific molecule can be labeled with some fluorescent marker (usually carbon 14). This type of marking allows the researcher to make observations about the movement of these molecules, as you can see in the question above. About the research shown in the question, the researcher realized that the protein labeled with the fluorescent marker moved between the grana and was always in the lumen, so she can conclude that the selocomovement protein moved through the lumen that is shared between the tilacoid membranes and the grana.
Antagonsitic effect/interaction/response
In order to combat antiobiotic resistance, and to possibly enhance the activity of antibiotics, they are sometimes used in combinations during treatment. However, three possible responses or effects can manifest.
First is antibiotic synergy, where the combined effect of the antibiotics enhances the activity/potency of the treatment compared to when the antibiotics are administered singly.
The effect is also distinguished from another type of response, which is additive effect, where the combined effect of the antibiotics is more or less equal to the combined activity/potency of each of the antibiotic when applied singly. Antibiotic synergy results in even greater enhancement of the activity of the combined antibiotics compared to additive effect.
Lastly, there is the antagonistic effect or response, where the combined effect of the antibiotics results in the weakening of the potencies of the antibiotics relative to the combined (additive effect) potencies of each of the antibiotics.
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:
Answer:
B. sheet of connective tissue that attaches a muscle to another muscle or bone.
Explanation:
The aponeurosis are mainly made of collagen fibers and works as an insertion to some skeletal muscles. The aponeurosis fibers can connects muscles to the bone or with another muscles connecting the aponeurosis fibers among themselves.
