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nignag [31]
2 years ago
11

Which descriptions represent social consequences of sustainable land use?

Biology
1 answer:
Zina [86]2 years ago
6 0

Answer:

II and III

Explanation:

Did the quiz : ()

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Why are G protein only found in Eukaryote cell ?
Levart [38]

Answer:

they bind to protein-coupled transmembrane receptors with higher complexity than those found in prokaryotes

Explanation:

G-proteins are proteins found inside the cells that function as molecular switches which are activated by binding to guanosine triphosphate (GTP), while they are inactive by binding to guanosine diphosphate (GDP). The G-proteins bind to G-protein-coupled transmembrane receptors (GPCRs) in the cytoplasmic region. The GPCRs are a very diverse group of proteins that are activated by extracellular molecules ranging from small peptides to large proteins, including pheromones, neurotransmitters, light-sensitive compounds, etc, thereby allowing them to respond to diverse stimuli from the extracellular environment. In consequence, it is reasonable to suppose that the signaling pathways in which G proteins are involved have a higher complexity level than those observed in primitive prokaryotic organisms.

6 0
3 years ago
Can genetic mutations benefit an organism? Explain your answer.
pochemuha

There are several mutations that benefit the organism.A well known example is the antibiotic resistance developed by bacteria, which aid in their survival even when they are exposed to a given antibiotic. A single gene mutation in wild almond trees resulted in a variety that no longer synthesizes amygdalin.

7 0
3 years ago
Read 2 more answers
nucleotides, which are the building blocks of nucleic acids, consist of a phosphate group, a nitrogenous base, and a? A. lipid B
stiv31 [10]
I believe it's B. 5 carbon sugar
8 0
3 years ago
A cut parallel to the midsagittal plane would produce a ________ section. A cut parallel to the midsagittal plane would produce
Sedaia [141]
You can use all the words is good to it
3 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
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