The statement 'interactions of the hydrophobic and hydrophilic amino acids help to anchor the protein in the membrane' explains why protein folding is critical. This process is fundamental for the function of transmembrane proteins.
Protein folding refers to the process by which a polypeptide (i.e., a protein) adopts its final tridimensional 3D shape (conformation).
In a protein, some amino acids contain hydrophilic R groups, whereas other amino acids contain hydrophobic R groups.
During protein folding, hydrophobic amino acids are arranged so they can interact with the long chains of the fatty acids in the internal region of the lipid bilayer, whereas hydrophilic amino acids are arranged so they interact with water on the surface of the cell membrane.
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<span>1)archaebacteria lack peptidoglycan of eubacteria
2)different membrane lipids
3)archaebacteria have different DNA sequences</span>
Answer:
D) Because sticky ends can be temporarily held together by hydrogen bonding between the two strands.
Explanation:
Restriction enzymes cut the DNA at specific restriction sites and by the mechanism of action they can form two types of ends:
- sticky ends-single-stranded overhangs are formed
- blunt ends-without overhangs.
The main advantage of sticky ends (their overhangs) is that they can complementary bind to another overhand formed by the same restriction enzyme. So, for example in cloning, if the DNA of interest and plasmid vector are cut with the same restriction enzyme, that forms sticky ends, fragment of DNA will fit into a bacterial plasmid in one direction.
On the other hand, blunt ends can be inserted into vector in both directions: head-to-tail or tail-to-head.
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