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Svetllana [295]
2 years ago
14

What event at letter b leads to elongation of the bone?

Biology
1 answer:
liraira [26]2 years ago
4 0

The occasion at letter b leads to elongation of the bone: <u>Ossification </u><u>of the epiphysis of a protracted bone.</u>

<u />

Elongation is defined because the period at the breaking point is expressed as a percent of its authentic duration (i.e. length at relaxation). If a rubber reaches two times its length earlier than breaking its elongation percentage is a hundred%.

Ultimately, elongation--the addition of nucleotides to the brand new DNA strand--starts offevolved after the primer has been brought. Synthesis of the developing strand entails adding nucleotides, one at a time, inside the actual order distinctive by using the authentic (template) strand.

Learn more about Elongation here:

brainly.com/question/26809816

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What major organelle are prokaryotes missing that eukaryotes have?
djyliett [7]

Answer:

Nucleus

Explanation:

Prokaryotes are the organism that came earlier than eukaryotes on this earth. These prokaryotes do not have a nucleus and other membrane-bound organelles like chloroplast, mitochondria, Golgi apparatus, endoplasmic reticulum, etc.  

So as prokaryotes lack membrane-bound organelle their genetic material is not enclosed in the nucleus therefore their genetic material remains in the cytoplasm of the cell while eukaryotes have membrane-bound nucleus in which their genetic material are present.  

So the nucleus is the major organelle that prokaryotes are missing that eukaryotes have.

4 0
3 years ago
Euglena use chloroplasts to make food through the photosynthesis process. <br> a. True<br> b. False
Elodia [21]
True

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3 years ago
Which of the following is an example of chemical weathering
Ludmilka [50]

Answer:

b

Explanation:

7 0
3 years ago
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8 0
4 years ago
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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
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