Can you help me with this problem set?
1. Explain how the empirical result that protein structures are composed of a limited number of domain structure motifs provides an approach to solving the Levinthal Paradox.
2. Provide a simple calculation explaining how the fact that most amino acid residues within globular proteins fall within a-helices or ß-strands sets an upper limit for the number of domain structure motifs that one expects to find in the totality of globular protein structures.
3. There are two schools of thought regarding the nature of the major driving force for protein folding. One holds that the major force is derived from formation of intrachain hydrogen bonds. The other holds that it is the hydrophobic effect that is the dominant driving force. Summarize the experimental evidence for each position.
4. Describe an example of an enzyme active site containing a group of amino acid residues that destabilizes the overall structure of the enzyme, and explain why this is so.
5. Explain why in studies directed toward evaluating the importance of a particular side chain for enzyme catalysis, the residue in question is typically mutated to an alanine rather than a glycine.