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MCAT
Course: MCAT > Unit 9
Lesson 9: Amino acids, peptides, proteins- Amino acids and proteins questions
- Central dogma of molecular biology
- Central dogma - revisited
- Amino acid structure
- Peptide bonds: Formation and cleavage
- Special cases: Histidine, proline, glycine, cysteine
- Isoelectric point and zwitterions
- Classification of amino acids
- Four levels of protein structure
- Conformational stability: Protein folding and denaturation
- The structure and function of globular proteins
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Classification of amino acids
Amino acids can be classified according to their side chain's chemical properties (the R-group). This video will show you how! By Tracy Kovach. Created by Tracy Kim Kovach.
Want to join the conversation?
- Would you recommend memorizing all 20 amino acids, their structures and their classifications for the MCAT?(30 votes)
- You should be able to classify all the amino acids by polarity, charge, aliphatic vs aromatic, and probably learn the structures and functional groups of the special amino acids (for example: two cysteines close in space may form disulfide bridges under oxidizing conditions, prolines tend to introduce kinks in polypeptides and are often found at the beginning of alpha helices).(82 votes)
- Why are non-polar molecules hydrophobic? I mean, they do not have any partial charge in their structure, thus neither attraction nor repulsion will occur.
Then why is it hydrophobic?(13 votes)- Well you're right that non-polar things will not have any attraction or repulsion with water. It's not that water doesn't like oil, it's that water doesn't like oil as much as it likes other water (or other polar molecules that act like water).
Each water molecule will try to lower its energy state by maximizing its number of hydrogen bonds with other polar molecules. This is seen at the macroscopic level as oil getting pushed away so that water can maximize the amount of polar-polar bonds.(13 votes)
- I was taught that tryptophan is a polar molecule due to NH bond next to the aromatic making it slightly polar. Your video seems to say otherwise. So is tryptophan polar or non polar?(6 votes)
- You're right, it would be slightly polar. However, since it is not strongly polar, tryptophan is still generally classified as having a nonpolar R group.(15 votes)
- At, she says that she remembers that the amino acids are basic because they have N atoms. So why aren't Proline and Tryptophan also polar/basic? 5:51(6 votes)
- The three amino acids are Lysine, Arginine, and Histidine, and how I remember these three is using the abbreviation for the strong base LAH (lithium aluminum hydride). They are basic because their side chain is basic and are positively charged at pH values below their pKa’s. Only the guanidine group (HNC(NH2)2) in Arg (pKa = 12.5) and amine group in Lys (pKa = 10.5) will accept a proton and exist with an overall charge of +1 at physiological pH. The imidazole group (ring structure with two N’s) in His (pKa = 6.0) would exist predominantly in neutral form.
Proline is not polar and basic because the N is not from the side chain. Proline originates from glutamic acid, the carboxy reduced to an aldehyde, amino group attacking to form the Schiff base, and further reduction. Basically, the N is from the original alpha-amino group. Proline qualifies as nonpolar and cyclic. As for tryptophan, it has an indole substituent on the beta-carbon. The N in the indole group (2 ring structure with one N) has no free lone pair to act as a base because it is already participating in the resonance. Tryptophan qualifies as nonpolar and aromatic.(14 votes)
- Atshe says she remembers polar amino acids by the presence of an oxygen or a sulfur atom in their side chains, but at 4:36, she says methionine is a nonpolar amino acid, even though there is a sulfur atom in its side chain. How are we supposed to recognize the difference between those? Is there another way to identify which are polar and which are nonpolar? 2:26(5 votes)
- Methionine contains a sulfur atom in its side chain, but it is surrounded by three carbon atoms. Cysteine, however, is only bonded to one carbon atom and one hydrogen atom. In methionine, then, there is certainly polarity in the molecule, but overall, the three carbons (and their hydrogen atoms) are more significant. When a molecule of some substance mixes with water, it disrupts the hydrogen bonding between water molecules. For very polar molecules, this isn't a problem, because they can interact strongly with water. For only weakly polar molecules, the energy "payoff" of bonding with water isn't enough to compensate for the disruption in water hydrogen bonding. You can see this effect with alcohols of different sizes; small alcohols like methanol and ethanol are miscible with water because they are strongly polar (-OH group attached to only one or two carbon atoms). Larger alcohols (propanol or hexanol) are not miscible with water because even though they are technically polar, they have such large hydrocarbon chains that they can't interact favorably with water, despite the hydroxyl group.(11 votes)
- I'm confused. In the books I'm reading, Basic Medical Biochemistry by Lieberman et al, and Lippincott's Biochemistry, Tyrosine is classified under aromatic amino acids, making it nonpolar like Tryptophan and Phenylalanine. They also say that Tyr and Try are more polar than Phe, but they still are relatively nonpolar. Can anyone help me understand? 4:38(7 votes)
- Tyrosine's phenol group can indeed hydrogen bond with water, but it can also energetically-favorably pi stack with surrounding aromatic amino acids (similar to DNA nitrogenous base stacking), typically within a protein's hydrophobic core. In fact, tyrosine pi stacking is commonly observed in known protein structures, and possibly more often than exposed tyrosines hydrogen bonding with water at the protein surface.(6 votes)
- Do amino acids in a low pH solution always have a positive charge?(4 votes)
- The word "always" is very difficult in biological science. But in most cases of extremely low pH (1-2) then yes all of the amino acids would carry a positive charge.(9 votes)
- What are aliphatic amino acids?(5 votes)
- Oil is an example of Hydrophobic, isnt it?(3 votes)
- Yes, oil is a non-polar molecule and so it will not mix with water, which is a polar molecule. This makes oil hydrophobic ("water fearing") and is why oil floats on top of water.(7 votes)
- At, Tyrosine is included as a Polar aa (also the side box says that it can be included as an aromatic acid. My question then is, is Tyrosine considered both non polar and polar amino acid then? My Kaplan textbook only shows tyrosine as an aromatic. 4:38(3 votes)
- I am not sure what is the right answer because I have been finding conflicting answers. This source says tyrosine is polar: http://www.thinkpeptides.com/aminoacidproperties.html. While this source says tyrosine is non-polar: http://www.biology.arizona.edu/biochemistry/problem_sets/aa/Tyrosine.html(3 votes)
Video transcript
All right. So let's go through the
classification of amino acids. And I've highlighted the word
class within classification for you, because
I'm going to paint for you a picture
of a classroom that is full of 20
different amino acids. And just picture this as
the most diverse classroom you've ever seen, because
each amino acid has their own unique
side chain, and this makes them distinctly
different from the amino acid next to them. And just like a real
classroom full of kids, even though each amino
acid is unique and special in their own way,
you can start to see that some of these
amino acids are more alike than
they are different. And we can start to
see these similarities in the chemical properties
of the side chains, and this allows us to
group them together into various categories. And those chemical
properties include the charge of the side chain, the
ability of the side chain to undergo hydrogen bonding,
and also whether or not we can classify that
side chain as being either acidic or basic. So the 20 amino acids
can be split broadly into kind of two main groups. The first group includes
the nonpolar amino acids, and then the second group
includes the polar ones. And the nonpolar
amino acids can also be thought of as the
hydrophobic, or water-fearing, amino acids. And conversely, you
have the polar ones. Those can be
considered hydrophilic, meaning water-loving. And yet another way that
I like to kind of think about these two main groups are
the hydrophobic amino acids-- they're kind of like
the water-haters. They don't really want to
interact with water at all. They'd rather just
interact with themselves. Whereas the
hydrophilic amino acids are very open and welcoming to
interacting with water, and so they're water-lovers. And then within the two
groups of nonpolar hydrophobic and polar hydrophilic
amino acids, you then have a further
breakdown into subgroups. And those subgroups
include those amino acids that have alkyl side chains,
aromatic side chains, neutral ones, acidic
ones, or basic ones. So let's take a closer look
at those amino acids that have alkyl groups
as side chains. And as you can see here, we have
seven different amino acids, and I've just drawn out
the side chain for you. I've left the rest
of the molecule out just to fit
everything in here. And we have glycine, alanine,
valine, methionine, leucine, isoleucine, and proline. And proline is the exception. I've drawn out the
entire amino acid there, because as you can
see, its side chain forms this interesting ringed
structure with the amino group in the backbone of the molecule. So I just included it
there for completeness. So all these side chains
are made up of alkyl groups, with the one exception
being glycine, because its side chain has
only a hydrogen atom in it. But because it behaves similarly
to an alkyl chain side group, it gets slumped into this
category of amino acids. And whenever you
see an amino acid with an alkyl group
as its side group, you should be thinking that
this amino acid is nonpolar. And so they're also
going to be hydrophobic. Now, let's take a closer look
at those amino acids that have aromatic groups as part of
their side chain, and remember, we're still under the umbrella
of nonpolar hydrophobic amino acids here. And so I've drawn out for
you here two amino acids, phenylalanine and tryptophan. And what should you
be thinking when you're looking at
these amino acids? So besides thinking,
oh, those amino acids must smell really
good, because they're called aromatic amino acids--
well, that might be true, but you should also be
thinking the same thing that you think when
you see amino acids with alkyl groups as
their side chains. These amino acids
that you see here are also nonpolar
and hydrophobic. And that kind of makes sense,
because aromatic chains are also just made up of
carbons and hydrogens. And you weren't wrong if you
thought that aromatic compounds might smell really good, because
many of our most aromatic herbs and spices that we're all
familiar with, like basil or cinnamon and
vanilla, are composed of the same sorts of ring
structures that we see here. All right. So now that we've tackled the
nonpolar hydrophobic amino acids, let's dive on into the
polar and hydrophilic amino acids. The first group that we will
look at is the neutral group. Here we have serine, threonine,
asparagine, glutamine, cystine, and tyrosine. The way that I remember that
these are the polar amino acids is that these amino acids
have a side chain that contain an oxygen
or a sulfur atom, which tends to hog all
the electrons around them to create a localized
negative charge over that atom and then a positive charge over
the rest of the side chain. So you can kind of see
why these amino acids like to hang out with water
now, since water is also polar in the same way. And these amino acids
are considered neutral, because although they are polar
enough to interact with water, they're not strongly
polar enough to qualify as an acid or a base. So which of the polar
hydrophilic amino acids do qualify as acidic? Well, that would be these two
amino acids here, aspartic acid and glutamic acid. As you can see,
these amino acids have a carboxylic acid as
part of their side chain, which is a very willing,
strong hydrogen donor which qualifies these amino
acids as acidic. When these side chains
do donate their hydrogen and they're left in anion
form, then in that case, we refer to them as aspartate
and glutamate, respectively. So you might see them
referred to in that way. Last but not least, we
have the basic amino acids, and they're histidine,
lysine, and arginine. And the way I remember that
these amino acids are basic is that if you take a closer
look at their side chains, you see a few nitrogen atoms. And remember that nitrogen is
a very willing proton accepter, and this is why they
qualify as basic.