Answer:
Cellulose is held by beta 1,4-glycosidic bonds making it linear while Glycogen is held by an alpha 1,4-glycosidic bond making it highly branched.
Explanation:
Cellulose and Glycogen are both carbohydrate polysaccharides formed from glucose monomers. According to the question, cellulose is a tough, fibrous, and insoluble (in water) polymer found to play a structural role in plants' cell wall while Glycogen is another polymer obtained from muscle or liver and disperses readily in hot water to make a turbid solution.
Although these two polysaccharides (cellulose and glycogen) are linked by (1, 4)-glycosidic bonds but the glucose monomers in CELLULOSE are linked by a beta 1,4-glycosidic, hence, making it a straight or linear polymer
GLYCOGEN, on the other hand, is linked by an alpha 1,4-glycosidic bond making it an highly branched polymer. This structure is responsible for the different physical properties of the two molecules.
Answer:
True
Explanation:
The Drosophila like the mammals possess X and Y chromosomes but as in males in which the XX is female and XY is male, the sex In Drosophila is not determined by the presence of Y chromosomes as a male determining factor are present on the autosomes.
However, the Y chromosome is important for males as they are involved in the formation of the sperms therefore the presence of Y is important. In the given question if the allele is present ion the Y chromosome which can reduce the size therefore the allele is passed on to the males only ans no females.
Thus, true is the correct answer.
the fly is female (Bridges 1921, 1925). Thus, XO Drosophila are sterile males. In flies, the Y chromosome is not involved in determining sex. Rather, it contains genes active in forming sperm in adults.
Physical or mental defects (such as cerebral palsy) can occur
Because some problems are not always small enough for one nation that can do it by themselves and need more helpo
Answer:
A 22 to 25 amino acid sequence present in the central section of the protein, which gives rise to an alpha helix in the membrane is known as the stop-transfer anchor sequence. The sequence plays an essential function in targeting the protein towards the plasma membrane. On the other hand, it also ceases targeting of the protein towards the endoplasmic reticulum, which was started by the signal peptide.
Thus, the process of translation of the remaining of the protein occurs within the cytosol due to the tethering of the transmembrane domain. In the stop-transfer anchor sequence, the hydrophobic amino acids present are isoleucine and valine. After mutation, these amino acids get converted into arginine and lysine, thus, hydrophilic amino acids replace hydrophobic amino acids in the sequence.
Due to this, the transmembrane domain cannot be targeted towards an integral part of the plasma membrane by the short transfer anchor sequence, and therefore, now the translocation of the protein will take place towards the endoplasmic reticulum as initiated by the signal peptide at the beginning.
