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Amino Acids

(Chapter 37B)
General Structures
 Two contrasting
groups
 -COOH acidic COOH
 -NH3 basic α
H 2N C H
 α-amino acids
 ~20 different α- R
amino acids
found in protein
in nature
Some amino acids

COOH COOH COOH


H 2N C H H 2N C H H 2N C H
H CH3
CH2COOH
Aminoethanoic 2-Aminopropanoic
acid Aminobutanoic acid acid
(Glycine) (Aspartic acid) (Alanine)
Chirality
 L-amino acid COO-
 Look down at
H-C bond,
other groups, C R
read clockwise H3N+
(‘corn’ law) H

eye
Special features
 High m.p. and b.p.
 Glycine (R=H) is a COO-
solid
+
H 3N C H
 Soluble in water
 High dipole moment R
Dipolar Ion
 Less acidic and basic (Switterion)
than normal RCOOH
and RNH2
Amphoteric
COO-
COO- As acid H2N C H + H3O+
H3N
+
C H R
R As base
COOH
+ H2O
+
H3N C H + OH-

R
Isoelectric point

COO- COO- COOH


OH- H+

H2N C H H3N C
+
H +
H3N C H
H+ OH-

R R R
(II) (I) (III)

pH at which the concentrations of (II) = (III)


is called the isoelectric point.
Separating amino acids
 Chromatography
Separating amino acids
 Electrophoresis
Peptide Linkage
H H H
O O
H3N+ C C H N+ C C
O- O-
R H R’
-H2O

H O H H
O Peptide linkage
H3N+ C C N C C (A Dipeptide)
O-
R R’
Proteins
 Polypeptides
 About 20 H O H H O
amino acids HN C C N C C
 Number of R R’ n
possible
protein
polymers is
very large
Proteins