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Backbone of polypeptide chain is polar or hydrophobic

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Reference no: EM133261400

Question 1.

Would you say that the backbone of the polypeptide chain is polar or hydrophobic? How then is it energetically feasible for the backbone to be folded into the interior of a protein?

Question 2.

Think about how many different values a dihedral angle pair can take, and then think about how many amino acids there are in a typical protein. What can you say about the possible number of distinct folds of a typical protein? What does Levinthal have to say about this? Do proteins fold by sampling all the possible conformations and then choosing the one with the lowest free energy?

Reference no: EM133261400

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