A2 Chemistry
Amino Acids
and
Proteins
Press “Esc” key to escape from any
presentation and return to previous menu
- AMINO ACIDS
= bifunctional compounds
amino group (-NH2) andacid group, (-COOH)
bonded to same C atom
General structure:
“R” = H
R Aminoethanoic acid
H
(glycine)
HO C C N:
“R” = CH3
H
O H 2-aminopropanoic
acid
(alanine)
Note: 20 different amino acids occur in nature.
All α-amino acids except glycine are optically active
4 different groups bonded to chiral C atom
non-identical mirror images = optical isomers / enantiomers
COOH HOOC
C C
H H
H2N NH2
R R
Isomers show equal but opposite rotation of plane-polarised light
More details
Equimolar mixture = racemate / racemic mixture
Racemate is optically inactive since rotations cancel
(Note : In nature, only one optical isomer occurs)
NINHYDRIN REACTION
O
OH
Ninhydrin =
OH
O
Used as a test for the presence of any amino acid
especially for locating amino acids after paper chromatography.
More details
Heat
Ninhydrin + Amino Acid Purple / blue compound
Note: Ninhydrin is used to detect fingerprints since skin
secretions contain amino acids.
Acid-Base Properties of AA
Acidic -COOH + basic -NH2
react with both acids and alkalis (i.e. amphoteric)
act as natural buffers –
absorb added acid / alkali to maintain pH.
R
H
In acid HO C C N: In alkali
+ H+ + OH-
O H H
R R
H H
+
HO C C N: H -
O C C N: + HOH
O H H O H H
e.g. present in excess HCl(aq) e.g. present in excess NaOH(aq)
NB At a particular pH (the isoelectric pH)
and in the crystalline solid,
amino acids exist as the zwitterion
(also called amphion)
where the proton (H+) has transferred
internally from -COOH to -NH2
R NB Isoelectric pH varies
- : + as R changes
HO C C N H can identify each AA
by its isoelectric pH
O H H value
Amino
Zwitterion
acid
During electrophoresis, an amino acid at its
isoelectric pH will NOT move in the electric field.
Polymerisation of 2-Aminoacids polypeptides
R H
Many (n) AA linked by
n HO - C - C - N repeated CONDENSATION
reactions – H2O eliminated.
O H H
PEPTIDE
BOND Hydrolysis of peptide bond
- catalysed by acid or alkali
R H R H R H
- C - C - N - C - C - N - C - C - N
etc etc
O H O H O H
Repeat unit + (n-1) HOH
Q Draw the structures of the dipeptides (polypeptides composed of sequences
of TWO amino acids derived from glycine (R=H) and alanine (R = CH3).
H CH3
HO C C N C C N H
O H H O H H
CH3 H
HO C C N C C N H
O H H O H H
Peptide bonds are hydrolysable
i.e. polypeptide + (n-1) H2O n amino acids
biodegradeable / digestible
(a) The amino acids can be separated and identified by
acid-catalysed hydrolysis [reflux with HCl(aq)], followed
by paper chromatography.
(b) Partial hydrolysis to a mixture of dipeptides and tripeptides,
followed by paper chromatography, can also allow the
sequence of amino acids in a polypeptide to be deduced.
(b) the “primary structure” of a polypeptide.
AA1 AA2 AA4 AA3 AA3 AA2
or AA2 AA1 AA1 AA3 AA3 AA4
etc
PROTEINS
Polypeptide (fixed sequence of amino acids = primary (1º) structure)
(a) coiling of 1º chain
or (b) folding of 1º chain
Secondary structure = (a) an α-helix Both shapes
maintained by
or (b) a β-pleated sheet internal H bonds
Folding and bending of 2º structure
Shape maintained by VW
Tertiary structure = overall 3D forces, ionic linkages,
shape of protein hydrogen bonds and / or
disulphide bridges
Possible association with
non-polypeptide substance
Quaternary structure
NB Each protein has its own unique P, S, T and Q structures
The End
POLARIMETRY
θ
Amino
acid in
Single Plane solution Rotated
wavelength polarised plane
light light polarised
light ROTATABLE
FIXED polaroid
polaroid
= “polariser”
= “analyser”
Analyser measures direction and amount of rotation
eg θ in clockwise direction
Clockwise called DEXTROROTARY (d) amino acid
Anti-clockwise called LAEVOROTARY (l) amino acid
BACK
Note:
Spots only
Chromatography
visible after
paper
location by
ninhydrin.
X
Spot containing
mixture of amino
dS dX acidsfor analysis
Solvent
Distance moved by amino acid X
Rf of amino acid X =
Distance moved by solvent
=
dX
dS BACK
HELICAL SECONDARY STRUCTURE
Side chain
O atom
HYDROGEN BOND
C atom
H atom
N atom
RETURN
β-PLEATED SHEET SECONDARY STRUCTURE
Folded polypeptide chain
HB Folded polypeptide chains linked into
sheet by hydrogen bonds (HB)
RETURN
TERTIARY PROTEIN STRUCTURE
Van der
Waal
forces
Primary &
secondary
structure
H-Bond
Disulphide bridge
Ionic Bond
RETURN
QUATERNARY PROTEIN STRUCTURE
e.g. Haemoglobin
Haem group
4 Primary,
secondary &
tertiary coils
RETURN
