Lesson Learning Outcomes

Upon completion of this lecture,

students should be able to:

 understand the structures and

properties of amino acids
 know the groups of amino acid
What are amino acids?
 Amino acids are molecules that when combined with
each other  proteins.
 Amino acids contain a central tetrahedral carbon
atom (α-carbon)
 amine group, carboxyl group, R-side chain
 The R-side chain determines the different amino
acids
 There are 20 common amino acids
 Amino acids can join via peptide bonds
 Several amino acids occur only rarely in
proteins
 Some amino acids are not found in proteins
3D structure of amino acids
 Why is the 3D structure (stereochemistry) of
amino acids important?
 Amino acids appear in chiral (mirror image)
except for glycine where the R = Hydrogen
 Chirality of amino acids can only be seen in 3D
structure
 The position of amino group on the left or
right side of the α-carbon determines the L
or D designation.
 L-amino acids are found in proteins
 D-amino acids are often found in bacterial
cell walls and in some antibiotics.
 There are 20 common amino acids
 Amino acids can join via peptide bonds
 Several amino acids occur only rarely
in proteins
 Some amino acids are not found in
proteins
Amino Acids Can Join Via Peptide Bonds
 20 Common Amino Acids
 Non-polar amino acids
 Polar, uncharged amino acids
 Acidic amino acids
 Basic amino acids
(a) nonpolar (hydrophobic)
(b) polar, neutral
c) acidic
(d) basic
Several Amino Acids Occur Rarely
in Proteins
 Hydroxylysine, hydroxyproline - collagen
 Carboxyglutamate - blood-clotting proteins
 Pyroglutamate – in bacteriorhodopsin
 Phosphorylated amino acids – a signaling device
Isoelectric point
 Isoelectric point is the point along the pH scale
where the molecule (amino acid) exist in a
neutral form with a zero net charge
 Iso = equal
 Why is it important?
 So we can predict the charge of the amino acid
at a certain pH
 The general structure of amino acid:
 The general structure of amino acid:

• Proton
acceptor
• Makes it • Proton
basic donor
• Makes it
acidic
Amino acids can act as both acid
and bases
 Carboxyl group (-vely charged) and amino
group (+vely charged) of the general
structure – charged at neutral pH
 Amino acids that exist with a net charge of
zero is called - zwitterion
 What happens when an amino acid is placed in
acidic solution (lots of H+)?
 The amino group will accept the excess H+ and
form NH3 – positively charged
 The carboxyl group will also gain proton and
become uncharged
 Thus the amino acid will be positively charged
 What happens when an amino acid is placed in
basic solution (lots of oH-)?
 The amino group will be deprotonated the excess
oH- and form NH2 – no charged
 The carboxyl group will also be deprotonated and
become negatively charged
 Thus the amino acid will be negatively charged
Range of forms amino acid can make

The point on the pH scale that we

can find the zwitterion is what we
call the isoelectric point.
Spectroscopic Properties
 All amino acids absorb infrared wavelengths
 Only Phe, Tyr, and Trp absorb UV
 Absorbance at 280 nm is a good diagnostic
device for amino acids – useful for
detection of proteins contamination in dna
extraction
Separation of Amino Acids
 Mikhail Tswett, a Russian botanist,
first separated colorful plant pigments
by ‘chromatography’
 Many chromatographic methods exist
for separation of amino acid mixtures
 Ion exchange chromatography
 High-performance liquid
chromatography
Chromatographic fractionation of a synthetic
mixture of amino acids on ion exchange
columns
Read up Chapter 3