Section Bank C/P 94 HELP

[mynameisno]

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How do you know Position 232 is not involved in catalysis? Passage paragraph 1 states the amino acids that glycerol interacts with but 232 seems to be pretty close to Asp 246? Basically, why is C not a possibility?

 

[PositivePhotoresist]

May you please attach a picture?

 

[mynameisno]

May you please attach a picture?

Sorry I thought I did, I uploaded one!

 

[smukke]

C might be correct, there's nothing wrong with thinking that, however following that line of thought, why wouldn't A and D be possible too? We just don't have enough information given in the passage except that it supports B.

(Personally I would have been stuck between A and B)

 

[mynameisno]

C might be correct, there's nothing wrong with thinking that, however following that line of thought, why wouldn't A and D be possible too? We just don't have enough information given in the passage except that it supports B.

(Personally I would have been stuck between A and B)

What evidence would u say supports B?

 

[smukke]

What evidence would u say supports B?

The increased enzymatic activity based on the table.

Like I said in your other post, sometimes it's a matter of finder the better/best answer, even if the others could potentially be right.

 

[mynameisno]

The increased enzymatic activity based on the table.

Like I said in your other post, sometimes it's a matter of finder the better/best answer, even if the others could potentially be right.

Okay, thank you 🙂 That was my reasoning too cause it had similar activity as GK-P in the table but I wasnt sure if that was the right way to go about getting the answer...

 

[Flufpot12]

Why do you guys suppose A can’t be correct?

 

[Doogie.Howser]

Why do you guys suppose A can’t be correct?

The key to this answer is knowing that structure determines function. What allows GK-P to have higher activity is that the phosphorylation changes the shape of the enzyme itself, as stated in the passage. The activity of the H232R variant, and the other variants, are caused by the shape.

For answer A: interactions are important, don't get me wrong. Changing a positive group like H to a non-polar neutral group of A was shown to have a low activity. Why? Because it ultimately changes the shape of the enzyme.

 

[mynameisno]

The key to this answer is knowing that structure determines function. What allows GK-P to have higher activity is that the phosphorylation changes the shape of the enzyme itself, as stated in the passage. The activity of the H232R variant, and the other variants, are caused by the shape.

For answer A: interactions are important, don't get me wrong. Changing a positive group like H to a non-polar neutral group of A was shown to have a low activity. Why? Because it ultimately changes the shape of the enzyme.

Ah okay so its like what is more right and B is more right because it directly deals with the root cause of the change in enzyme activity?

 

[Doogie.Howser]

Ah okay so its like what is more right and B is more right because it directly deals with the root cause of the change in enzyme activity?

B is more correct, yes.

Interactions --> structure --> function.

Interactions help form function, but ultimately it's structure that determines function.

Take sickle-cell anemia for example. A glu to val mutation in hemoglobin changes the interactions that make the protein fold to it's most stable form. There is a "new" more stable folding pattern due to the mutation that causes a change in structure. The function of carrying oxygen is varied because it's now a different shape. Myoglobin and hemoglobin have different binding affinities for oxygen because of their structure.

Overall, remember for that structure determines function.

 

[deleted853480]

The 232 site only gets phosphoralated and probably doesn’t interact afterward. Substituting the H for R increases the rate the enzyme moves just like phosphorylation of site 232 does on the wild type.