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KatRina [158]
3 years ago
15

Select each process that produces an increase in the entropy of the system: check all that apply. check all that apply. cao(s) +

co2(g) → caco3(s) hcl(g) + nh3(g) → nh4cl(s) co2(s) → co2(g) 2 so2(g) + o2(g) → 2 so3(g)
Chemistry
1 answer:
skelet666 [1.2K]3 years ago
5 0
2SO2(g)+O2(g)→2 SO3(g), here reaction entropy decreases as the number of gas moles decreases from reactions to products.
HCL(g)+NH3(g)→NH4CL(s), entropy decreases as molecules of gas are converted into solid.
CO2(s)→CO2(g), entropy increases as gas is formed from a solid.
Cao(s)+CO2(g)→Caco3(s), entropy increases as gas is converted into a solid.
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For the interaction between actin and myosin to produce the contraction to occur, there must be calcium, which after the contraction must be removed and the delivery and elimination of this ion is carried out by the combined work of the tubular-T system and the RS. The RS surrounds the myofibrils as a system of networks, one of them around the A-band and the other in the I-band, and where the two networks meet, at the junction of the A-and -I bands, the RS It forms a cistern. The RS controls the level of intracellular Ca2 + in the skeletal muscle, storing and releasing it. Initially the sarcoplasmic reticulum develops as an ER, but as the muscle differs it is enriched with specific proteins. Three proteins initially purified from the sarcoplasmic reticulum are, calcium ATPase (SERCA), calsecuestrin (CLQ) and ryanodine receptor (RyR). SERCA is responsible for pumping calcium into the RS light during relaxation, while CLQ is the most prominent of the calcium chelating intraluminal proteins and between them increases the capacity of the RS for calcium. The most abundant SR protein outside the tubule-T-RS junction is SERCA, which is normally distributed in tubular elements surrounding the Z-and -M lines, as well as in the elements aligned with the longitudinal axis of the myofibril. In the light of RS the most abundant protein is CLQ, an acidic protein that binds calcium with moderate affinity and high capacity.

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