2014 P3 Q4
I still dont get it. Why only coo- group of aspartic acid can
interact with the amino acid di) residue given by the qn
Val and tyr aren't polypeptide chains, their discrete amino
acids
Aren't the groups on val and tyr considered R groups?
Aspartic acid's R group is a COO- group. Valine's R group is an
alkyl group. Tyrosine's R group is a phenol group. The question
isn't asking for interactions between discrete amino acids. It's
asking for interactions between R groups of these amino acid
residues within a polypeptide chain. Don't lose your marks
carelessly like this, it'll cost you at least 1 grade (with steep
bell-curves).
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Update
Is my understanding correct, and can help improve my
explanation?
Sian, think question interpretation might also be a problem
Is it because :in this qn, the amino acids are part of a
polypeptide chain, e.g. val-tyr-asp- etc etc
Then, both val and tyr's nh2 and cooh is used up in amide bond
linkage
Only aspartic acid has the extra cooh group, hence can interact
with the qn?
But then wouldnt it be Hbond interactions?
I thought of another :
Is it because ph 7, so means its in water? ( thats why the acid
and basic group will deprotonate and protonate??)
Thats why will have ionic interactions instead of h bonding?
But if its in water, then hydrolysis would occur, then
wouldnt the nh2 and cooh group on val and tyr able to interact?
?
Help!
1st of all, hydrolysis only occurs partially, it's an acid-base
*equilibrium* remember?
2ndly, technically (Singapore JCs don't teach this well so it's not
surprising JC students don't really understand this), while COOH
and NH2 groups are only capable of (both donating and accepting) H
bonds, COO- and NH3+ groups are actually capable of participating
in both H bonds (COO- can only accept H bonds, while NH3+ can only
donate H bonds) as well as ionic bonds, depending on who the other
party is.
And yes, Cambridge expects you to automatically first deprotonate
COOH groups at pH7, and protonate NH2 groups at pH7.
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If ph7 in water, will it cause the polypeptide chain to
undergo hydrolysis and cause it to break into small portions of
amino acid residues?
Oi!!! Wah biangz eh, if at pH7 and room temperature, proteins
spontaneously "break into small portions of amino acid residues",
then you won't be able to remain in 1 piece typing this post with
your phone liao (you won't even be able to hold your phone), you'll
disintegrate instantly into a sludge. Sludge
man!
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Can tyrosine's phenol group interact with nh3+?
If cannot, is it because phenol doesn't ionise in water?
Hydrogen bonding is possible, between the partial positive H atom
of NH3+ (the H bond donor), and the partial negative O atom of
phenol (the H bond acceptor).
Cambridge already stated in the question, regarding extent of
deprotonation of phenol at pH 7. Read the question carefully
lah!