Please evaluate the correctness of these responses:? 1. a) Describe the initial
ID: 282163 • Letter: P
Question
Please evaluate the correctness of these responses:?
1. a) Describe the initial stages of protein folding that create the molten globular intermediates Protein folding is driven by the hydrophobic effect, which causes the nonpolar regions of the amino acid sequences to collapse into the core of the protein, and the polar regions to face the outside. The hydrogen bonding between the polypeptide backbone and water is replaced by hydrogen bonding in secondary structures Molten globular intermediates are initially formed as the protein undergoes different folding conformations. The protein attempts different folding conformations until it achieves its native structure b) Why do 20 structures form as a protein folds? Secondary structures form when a protein folds because the secondary structures replace the hydrogen bonds lost between the polypeptide backbone and water. The parts of the protein which lose hydrogen bonding with water are now in the core of the protein and exposed to hydrophobic molecules c) List the types of interactions that cause the multiple globular intermediate forms to rearrange to a single native structure? 1) Hydrophobic effect of the side chains of amino acids. 2) Hydrogen bonding of the polypeptide backbone. 3) Electrostatic forces of side chains d) What is the general function of chaparones and chaparonins? Chaparones and chaparonins assist in the folding of proteins into their native structure e) What is the specific function of PDI? PDI assists in the shuffling of disulfide bonds between Cys residues. Both an oxidizing and reducing agent, PDI will reduce and break disulfide bonds if a protein misfolds. However, PDI will oxidize and form disulfide bonds in promoting a protein to fold into its native structure 2.Explanation / Answer
All the questions answered are correct.
They are correctly answered and represented in an organized manner. In my point of view, they are correctly represented.