Answer:
C. glycosylation
Explanation:
The maturation-promoting factor (MPF) is a cell cycle checkpoint that stimulates the passage from G2 (prophase) to M phase (metaphase). MPF also determines that DNA replication during the S (synthesis) phase did not produce any mutations. MPF is inactivated by kinase phosphorylation and activated by specific phosphatases capable of dephosphorylating this protein. On the other hand, glycosylation is a posttranslational modification where a carbohydrate (i.e., a glycan) is added to a functional group of another molecule. Many proteins undergo glycosylation, thereby playing a critical role in regulating protein function.
Answer:
- Glycine
- Ribulose 1,5-bisphosphate
- 3-phosphoglycerate
- Glyceraldehyde 3-phosphate.
- Glucose
- Sucrose
Explanation:
The glycine, among other amino acids, helps to improve chlorophyll production and promotes the process of photosynthesis.
<u>Calvin cycle</u>
During the carbon fixation phase, a CO² molecule combinate with a ribulose 1,5-bisphosphate to form 6-carbonated molecules, which will divide into two 3-phosphoglycerate molecules.
During the reduction phase, NADPH donates its electrons to reduce 3-phosphoglycerate molecules, and turn them into glyceraldehyde 3-phosphate.
During the regeneration phase, a glyceraldehyde 3-phosphate molecule leaves the cycle and goes to the cytosol to form glucose. This step can be done when three CO² enter the cycle and produce six glyceraldehyde 3-phosphate molecules. One of them leaves the cycle to form glucose, while the other five are recycled.
<u>Cytosol: </u>
Once in the cytosol, glyceraldehyde 3-phosphate molecules are used to form glucose and fructose. These two molecules are the monosaccharides that form the sucrose.
Once sucrose is formed, it is transported from the photosynthetic tissues to different parts of the plant by the phloem.
Yes very true because we are not bacteria
I think BO or B, but BO has more chance.
Answer:
as a dimer consisting of two identical monomers (80 kDa subunits) that are packed together via hydrophobic interactions
Explanation:
SDS-PAGE (sodium dodecyl sulphate–polyacrylamide gel electrophoresis), is an electrophoretic methodology used to separate proteins that have a molecular weight between 5 to 250 kDa. SDS is a well-known ionic detergent that is able to break hydrophobic interactions and hydrogen bonds. Moreover, size-exclusion chromatography is a filtration technique that separates molecules in solution according to their molecular size. In this case, SDS-PAGE showed that the target protein is composed of two identical subunits (monomers) of 80 kDa each, which were separated by the detergent and formed one single band in the SDS-PAGE gel.
