Biochemistry question from example paper Watch

naominaom1
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Describe the properties of hydrophilic amino acids that make it more likely to be found on the outside of a globular protein?

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this question was on a example paper and i have no clue how to answer it :/
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Reality Check
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(Original post by naominaom1)
Describe the properties of hydrophilic amino acids that make it more likely to be found on the outside of a globular protein?

4 marks
this question was on a example paper and i have no clue how to answer it :/
Well, think about the environment that this globular protein is likely to be found in. Globular = enzyme = cellular = AQUEOUS

So, from then, think about what sort of bonds and interaction these aa could make. H bonds, polar interactions.... You get the idea.

Have a look at the structure of serine compared with alanine, or threonine compared to valine. What do you notice about the structure of the R group, in particular the functional group(s) and how does that make serine and threonine more suited to interact with the aqueous environment?
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naominaom1
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(Original post by Reality Check)
Well, think about the environment that this globular protein is likely to be found in. Globular = enzyme = cellular = AQUEOUS

So, from then, think about what sort of bonds and interaction these aa could make. H bonds, polar interactions.... You get the idea.

Have a look at the structure of serine compared with alanine, or threonine compared to valine. What do you notice about the structure of the R group, in particular the functional group(s) and how does that make serine and threonine more suited to interact with the aqueous environment?
thanks
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Reality Check
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(Original post by naominaom1)
thanks
No problem. The corollary of this, obviously, is that hydrophobic aa's are to be found in the interior of the protein, shielded from the aqueous environment.
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