1. What type of secondary structure would a peptide composedonly of the amino acid Lysine form?
a) a random coil at all pH values
b) alpha helix at pH 7
c) alpha helix at pH well above 7
d) alpha helix at pH well below 7
2. During vigorous exercise ATP is hydrolyzed as follows,
ATP----> ADP +Pi + (H+)
what are the consequences of this for the structure-function ofhemoglobin?
a) hemoglobin binds O2 stronger as a result of the changingpH
b) lower pH results in deprotonation of His146 whichdestabilizes the ion pair between monomers
c) lower pH results in protonation of His146 which stabilizesthe ion pair between monomers
d) nothing happens to hemoglobin, only myoglobin isaffected.
3. If you were to make a mutation to hemoglobin so that it couldno longer form tetramers, what would you predict would occur.
a) impossible to predict
b) it would bind oxygen with lower affinity than before
c) it would transport oxygen better
d) hemoglobin would no longer be able to transport oxygen
