An organism that feeds on plant matter is a herbivore.
Answer:
The answer is unicellular
Answer:
3212
Explanation:
Transport vesicles are vesicles that function to carry molecules from one cellular compartment to another. The coat protein complexes I and II (COPI and COPII) are conserved pathways that transport proteins from the endoplasmic reticulum to the Golgi apparatus. Moreover, clathrin is a protein implicated in the formation of coated vesicles. The ADP-ribosylation factor GTPase activating (Arf GAP) proteins play a major role in Arf signaling pathways, which are responsible for uncoating of the COPI coat. On the other hand, COPII vesicles are known to retain their coats until they are recognized by tethering complexes, and whose formation is regulated by the GDP-GTP cycle of the small GTPase Sar1. Finally, the 70-kDa heat shock proteins (HSP70) are chaperones which function as uncoating ATPases to remove clathrin from coated vesicles after endocytosis.
<span>The answer is autosomes.
</span>In
a human diploid somatic cell (2n), there are 22 chromosomes
present in two copies and 1 pair of sex chromosomes. This means
there are 23 pairs of chromosomes - 22 pairs of autosomes and 1
pair of sex chromosomes. <span>There are in total 46 chromosomes (23 pairs
in 2 copies: 23 × 2 = 46).</span>
Answer:
they bind to protein-coupled transmembrane receptors with higher complexity than those found in prokaryotes
Explanation:
G-proteins are proteins found inside the cells that function as molecular switches which are activated by binding to guanosine triphosphate (GTP), while they are inactive by binding to guanosine diphosphate (GDP). The G-proteins bind to G-protein-coupled transmembrane receptors (GPCRs) in the cytoplasmic region. The GPCRs are a very diverse group of proteins that are activated by extracellular molecules ranging from small peptides to large proteins, including pheromones, neurotransmitters, light-sensitive compounds, etc, thereby allowing them to respond to diverse stimuli from the extracellular environment. In consequence, it is reasonable to suppose that the signaling pathways in which G proteins are involved have a higher complexity level than those observed in primitive prokaryotic organisms.