Question

1 mutation that is known to result in an inactive HGD enzyme replaces the proline at position 230 with serine. Determine why this mutation is likely to inactivate HGD.
“The mutation that replaces proline 230 with serine most likely results in an inactive HGD enzyme because the mutation:
1)disrupts an ionic or hydrogen bond within each individual subunit.
2)disrupts a hydrophobic interaction within each individual subunit.
3)changes an amino acid that is bonded with the iron atom at each active site.
4)disrupts an ionic or hydrogen bond that links different subunits to each other.

Answer 1

5) disrupts a hydrophobic interaction that links different subunits to each other.

Answer 2

Which is the correct statement? 1, 2, 3, 4, or 5?

Answer 3

i think 5 makes sense

Answer 4

I hope so... :-))

Answer 5

Not so sure on that one. What's your thought process?

Answer 6

I am confused as to what is right.

Answer 7

I have done a pretty detailed search of Google without luck. That serine is polar and uncharged but that proline is a mighty special molecule. That carbon ring is very hydrophobic... but check out the ionic bonding sites at both ends of the molecule. Frankly, I don't know the answer on this one... but it's not obvious to me that 5) is the answer.

Answer 8

The correct answer is the 2nd!

Answer 9

Really? I was betting on 4)

Answer 10

Really!