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a. Give the advantages and disadvantages of using NMR techniques to determine a proteins tertiary/quaternary structure.
b. Explain why a protein can not refold if the protein is first denatured, then the disulfide bonds are cleaved, then the protein is treated with excess iodoacetate or performic acid.
c. What can one infer about the number and kind of amino acids of a protein when the pI is greater than 7 and when the pI is less than 7.
d. Explain the difference between chaperones and chaperonins.
e. Describe the process by which proteins fold. Especially in regards to the difference between a local minimum and a global minimum.
f. Give the steps needed to determine a proteins primary structuref(A diagram or flow chart will work)
g. Explain the reasons why protecting groups are necessary when doing in vivo peptide synthesis?
Application Global Health.
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