Answer:
D. 4E-BP1 binding to elF4E prevents loading of the mRNA onto the ribosome.
Explanation
In eukaryotic organisms, the eIF4E translation initiation factor functions by directing the ribosomes to the 5'-terminal cap structure of the messenger RNA (mRNA) in order to start the translation. Moreover, phosphorylation is a posttranslational modification of specific amino acids on proteins that play diverse cellular functions by altering protein stability, location, and/or enzymatic activity. It has been shown that elF4E phosphorylation is increased in response to cellular stimuli that induce translation in the ribosomes (e.g., growth factors, hormones, etc). The eukaryotic translation initiation factor 4E (eIF4E)-binding protein 1 (4E-BP1) is a repressor of mRNA translation which is phosphorylated and inactivated by growth factors and hormones, thereby inhibiting 4E-BP1 binding to elF4E and consequently activating translation.
Answer:
d. Competitive inhibition will decrease because the proportion of the active sites occupied by substrate will increase.
Explanation:
Enzymes are bio catalysts in living cells responsible for aiding biochemical reactions.
Their active sites are primary protein 3D structure for binding with substrates during reactions.
Enzymes reactions are usually affected by inhibitors(e.g methyl alcohol) which compete with the active site with the actual substrate(ethyl alcohol) ,
This is an example of competitive inhibition. The more ethyl alcohol available, the more active sites occupied, therefore denying the inhibitor methylalchol chances to the active site, thus preventing the formation of toxic formaldehyde, and more of non toxic substances from formation of more ADH-METHYL ALCOHOL COMPLEXES at the active sites
Answer:
The fossils gradually drifted apart over a long period of time
Explanation:
Although a single human was not able to witness it since the earth's plates shift slowly, the fossils eventually seperated over the course of tens of millions of years.
I have no idea what you are talking 'bout.
