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swat32
3 years ago
6

In an experiment, researchers provided a radiolabeled amino acid to living plant cells. After one hour, the researchers determin

ed the amount of the radiolabeled amino acid that was in each of several subcellular compartments. The results of the experiment are represented in the table.
Biology
1 answer:
DIA [1.3K]3 years ago
3 0

Answer:

The correct option is B.<u> It was mostly incorporated into proteins that regulate and manage metabolic reactions.</u>

Explanation:

The results of the experiment showed that most of the radiolabeled amino acids were present in the mitochondria.

Amino acids can be described as organic compounds which build up the proteins. There are 20 different kinds of amino acids which make up different kinds of proteins, each specified to perform specific functions.

The results from the experiment prove that the radiolabeled amino acid is being used to make proteins that are necessary for metabolic reactions.

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<h3>How does penicillin affect bacterial cell walls?</h3>
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Using the sliding flament theory, explain (or draw) the process of sarcomere shortening. Start from the point where calcium woul
Arte-miy333 [17]

Answer:

  1. Calcium binds to troponin C
  2. Troponin T moves tropomyosin and unblocks the binding sites
  3. Myosin heads join to the actin forming cross-bridges
  4. ATP turns into ADP and inorganic phosphate and releases energy
  5. The energy is used to impulse myofilaments slide producing a power stroke
  6. ADP is released and a new ATP joins the myosin heads and breaks the bindings to the actin filament
  7. ATP splits into ADP and phosphate, and the energy produced is accumulated in the myosin heads, starting a new cycle
  8. Z-bands are pulled toward each other, shortening the sarcomere and the I-band, producing muscle fiber contraction.

Explanation:  

In rest, the tropomyosin inhibits the attraction strengths between myosin and actin filaments. Contraction initiates when an action potential depolarizes the inner portion of the muscle fiber. Calcium channels activate in the T tubules membrane, releasing <u>calcium into the sarcolemma.</u> At this point, tropomyosin is obstructing binding sites for myosin on the thin filament. When calcium binds to troponin C, troponin T alters the tropomyosin position by moving it and unblocking the binding sites. Myosin heads join to the uncovered actin-binding points forming cross-bridges, and while doing so, ATP turns into ADP and inorganic phosphate, which is released. Myofilaments slide impulsed by chemical energy collected in myosin heads, producing a power stroke. The power stroke initiates when the myosin cross-bridge binds to actin. As they slide, ADP molecules are released. A new ATP links to myosin heads and breaks the bindings to the actin filament.  Then ATP splits into ADP and phosphate, and the energy produced is accumulated in the myosin heads, which starts a new binding cycle to actin. Finally, Z-bands are pulled toward each other, shortening the sarcomere and the I-band, producing muscle fiber contraction.

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