Cannabinoid receptors, located throughout the body, are part of the Endocannabinoid system which is involved in a variety of physiological processes including appetite, pain-sensation, mood, and memory.[1]
Cannabinoid receptors are of a class of cell membrane receptors under the G protein-coupled receptor superfamily. As is typical of G protein-coupled receptors, the cannabinoid receptors contain seven transmembrane spanning domains.[5] Cannabinoid receptors are activated by three major groups of ligands: endocannabinoids, produced by the mammillary body; plant cannabinoids (such as Cannabidiol, produced by the cannabis plant); and synthetic cannabinoids (such as HU-210). All of the endocannabinoids and plant cannabinoids are lipophilic, such as fat soluble compounds.
Answer: D - Lipids
Lipids provide a long term energy storage because they contain longer C-H bonds compared to the other organic molecules, making it easier for them to store larger amount of energy. Moreover, upon burning they produce twice the amount of calories compared to that of the carbohydrates.
If a plant cell had a mutation such that the cyclic electron flow is observed at a much higher rate, which photosystem is most likely mutated such that energy is absorbed at a lower rate?
PSI
PSII
Answer:
PSII
Explanation:
Non-cyclic phosphorylation involves both PSI and PSII. The process starts with the splitting of water and excitation of electrons of the reaction center of PSII upon the absorption of solar energy at the wavelength of 680 nm. Any mutation in PSII would not allow the non-cyclic phosphorylation to occur when only cyclic phosphorylation would occur. The process of cyclic phosphorylation includes only PS I. Its reaction center absorbs maximum light at 700 nm and is cycled back while supporting ATP synthesis. Therefore, if a plant performs cyclic phosphorylation at a higher rate and absorbs less energy, this means that mutation was in PSII.
TRNA reads codons from mRNA and then brings attached amino acids accordingly. Amino acids are connected in long chains called proteins.
