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SULR as the fow thermometer un 2. When a protein denatures in a cell, what causes it to aggregate with other denatured cell p
7. How do molecular chaperones help newly synthesized proteins cross membranes? What evidence suggests that molecular chapero
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Answer #1

Question 2

When the protein denature in a cell, it means it looses the various type of bonds that were present in the 3D structure of the plant. When the protein get denature , protein is susceptible to misfolding or unfolding. When this denatured protein get interact with another denatured protein, they aggregate in which the hydrophobic group present in the R (side-chain) of amino acid may interact with exposed hydrophobic side chain of another amino acid.

Question 3

Heat shock protein are also known as Chaperons protein. These proteins help in the forming of correct bonds between the amino acid present in the newly synthesized polypeptide chain. The heat shock proteins stabilize the 3D structure of the protein by giving its correct binding between the side-chain of amino acid.

Question 4

The GroEL is a heat shock protein that give stability to the protein in high temperature conditions where protein could be denature easily. Similarly, the Rubisco is an enzyme that catalyze the first step of Calvin cycle and this enzyme is also very high temperature resistant enzyme and do not get denature at high temprtature.

Question 5

It is not suprising that two proteins present in prokaryotes and other in eukaryotes are so similar because all organism have evolved from one common ancestor. The prokaryotes have evolved first and eukaryotes later. But still there are many proteins that are similar in both group of organism because of common evolution.

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