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mariarad [96]
2 years ago
8

How do you think it is possible to create over 100 000 different proteins from just 20 amino acids?

Biology
1 answer:
never [62]2 years ago
3 0
<span>Protein is made up of building blocks called amino acids</span>
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<span>Toxic shock syndrome</span>
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Process in sexual reproduction in which male and female reproductive cells join to form a
harkovskaia [24]

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Fertilization

Explanation:

Fertilization is when an sperm cell fertilizes an egg cell

6 0
2 years ago
You wish to produce a human enzyme, protein A, by introducing its gene into bacteria. The genetically engineered bacteria make l
Blizzard [7]

Answer:

The options A, B, and D are all valid.

Explanation:

  • The reason is that some proteins require molecular chaperones if they are to fold properly within the environment of the cell. In the absence of chaperones, a partially folded polypeptide chain has exposed amino acids that can form non-covalent bonds with other regions of the protein itself and with other proteins, thus causing nonspecific aggregation of proteins.
  • The option A) is correct because the protein you are expressing in bacteria is being made in large  quantities, it is possible that there are not enough chaperone molecules in the  bacterium to fold the protein. Expressing the protein at lower levels might  increase the amount of properly folded protein.
  • The option B) is correct as urea should solubilize the protein and completely unfold it. Removing the urea  slowly and gradually often allows the protein to refold. Presumably, under less  crowded conditions, the protein should be able to refold into its proper  conformation.
  • The option C) is not correct as treating the aggregate with a protease, which cleaves peptide bonds, will probably  solubilize the protein by trimming it into pieces that do not interact as strongly with  one another; however, chopping up the protein will also destroy its enzymatic activity.
  • The option D) is correct because overexpressing chaperone proteins might increase the amount of properly folded protein.
  • The option E) is not correct as heating can lead to the partial denaturation and aggregation of proteins to form a solid gelatinous mass, as when cooking an egg white, and rarely helps solubilize proteins.

7 0
3 years ago
The membrane potential of a nerve cell will depolarize (become less negative) if there is an INCREASE in the __.
slava [35]

Answer:

The membrane potential of a nerve cell will depolarize if there is an increase in the positive ions inside the cell.

Explanation:

When nerves are in resting potential it is -70mV. In this stage interior of the cell is negatively charged and outside is more positive. When depolarization occurs the inside cell becomes positive.

This is due to the rush of sodium ions into the cell by voltage-gated channels. Now the inside charge is more positive and the chloride ions move out of the cell. Thus outside becomes more negative.

After some time of depolarization stage, potassium ions move out of the cell making the nerve cell again negative. Now the depolarized stage becomes repolarized by the entry of potassium ions.

During depolarization, the potential of the cell is -55mV.  When repolarization occurs, it is again -70mV. But the potassium channels are open and some of the potassium ions move out of the cell making the inside environment more negative. This is known as hyperpolarization condition.  

This hyperpolarization remains for a short period where action potential can't occur. This period is called the refractory period. Again potassium ions enter into the cell. This results in the resting potential of the neuron again.

6 0
3 years ago
What do you think makes an argument stronger? Explain 1- 2 things that would make an argument stronger and more believable?
OLEGan [10]

Answer:

a diagram, speech photos and classifications

Explan

3 0
2 years ago
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