AMINO ACIDS
Building blocks/stones of proteins
Fundamental sub-units of proteins
GENERAL FORMULA:
Carboxyl group = acidic properties
Amino group = basic properties
Chiral C = asymmetric carbon
PROPERTIES:
PHYSICAL:
1. White crystalline substances
2. Soluble in cold water, except cysteine and tyrosine which are more soluble in hot water
3. Insoluble in alcohol and ether except proline and hydroxyproline
4. All amino acids except proline are precipitated off from their solutions by alcohol, but
not by (NH4)2SO4 or NaCl
5. Most of them are sweet like glycine, alanine, serine ad proline, others like leucine are
tasteless; while some are bitter like arginine
CHEMICAL:
1. Amino acids are amphoteric due to the presence of both carboxyl and amino groups as
mentioned above. As such they form crystalline salts with metallic bases and with
mineral acids
2. Form esters with alcohol – by fractional distillation
3. Amino acids can be acetylated, benzylated or methylated in the presence of acetic acid,
benzoic acid or methyl group, respectively.
These reactions occur in the body during detoxication processes
4. All amino acids except proline and hydroxyproline react with nitrous acid with the
liberation of nitrogen gas.
This is the principle involved in Van Slyke method for determining amino groups in
proteins, blood and other biological substances
5. FORMALDEHYDE REACTION: When an excess of neutral formaldehyde is added to
neutral amino acid solution, a distinctly acid mixture is produced
The hydrogens of the amine group are replaced by a methylene group thus destroying
the basic property and allowing the carboxyl to assert itself freely
Subsequent titration with standard alkali measures the amount of the free carboxyl
groups.
Basis of Sorensen test
6. Amino acids form acyl halides
The amino group is previously protected by acetylation.
The protecting (-CO-CH3) group may subsequently be removed by using HCl
7. By heating with barium hydroxide, primary amines are formed due to the breaking off
the carboxyl group with formation of CO2
8. When amino acids are dehydrated, they unite with each other forming a ring, diketopiperazine
On boiling with HCl, diketopiperazine yields dipeptide
Fischer utilized this process in synthesizing polypeptides from amino acids
CHARACTERISTICS:
1. Optically active
All amino acids are optically active except glycine
Due to the presence of chiral/asymmetric carbon
Ability to rotate the plane p,arized light in a polarimeter
2.a. dextrorotatory (+) – plane polarized light shifted to the right
2.b. levorotatory (+) - plane polarized light shifted to the left
2. Amphoteric / ampholyte
Can act as an acid (proton donor) & as a base (proton acceptor)
COOH – proton donor (acid)
NH2 – proton acceptor (base)
3. Zwitterion / dipolar ion
Possesses both a positive or negative ion
Acidity is due to π electron delocalization. The OH bond in COOH weakens so it is
readily/easily given off or lost as a proton and is accepted by the lone pair in NH 3
4. Isoelectric Point (pI)
The pH value at which zwitterion state exists at a maximum
Amino acids & proteins assume a zero net charge
Amino acids & proteins are least soluble (ppt. form)
No integration in an electric field
Above pI : favors anionic state
Below pI : favors cationic state
Eg. Isoelectric Point (pI) :
Asp = 2.8 ala = 6.1
Glu = 3.2 lys = 9.7
Ser = 5.7 arg = 10.8
Val = 6
IMPORTANCE OF pI:
1. Used in buffer systems
2. For separation & identification purposes – since each amino acid has its distinct pI
3. Show structural changes in globular CHON – the explanation of structures of biological
reactions
5. ACID – BASE PROPERTY
ACIDIC
BASIC
CLASSIFICATION OF AMINO ACIDS:
I- ACCORDING TO R-GROUP
A. NEUTRAL OR STRAIGHT CHAIN AMINO ACIDS:
1. Glycine (gly) 2. Alanine (ala)
B. BRANCHED CHAIN AMINO ACIDS:
1. Valine (val) 2. Leucine (leu) 3. Isoleucine (ile)
C. ACIDIC AMINO ACIDS:
1. Aspartic acid (asp) 2. Glutamic acid (glu)
D. BASIC AMINO ACIDS
1. Lysine (lys) 2. Histidine (his) 3. Arginine (arg)
E. AROMATIC AMINO ACIDS
1. Phenylalanine (phe) 2. Tyrosine (tyr) 3. Tryptophan (trp)
F. SULFUR-CONTAINING AMINO ACIDS
1. Methionine (meth) 2. Cysteine (Cys or cys1) 3. Cystine (Cys or Cys2)
G. HYDROXY-CONTAINING AMINO ACIDS
1. Serine [Link]
H. IMINO ACIDS – not an amino acid because of the absence of NH 2 but only NH
1. Proline (pro)
2. Hydroxyproline (hpr)
II- ACCORDING TO IMPORTANCE:
A. ESSENTIAL / INDISPENSABLE AMINO ACIDS
Those which cannot be synthesized in the body
Must be provided in the diet
Primarily concerned with growth and maintenance of life
Examples:
1. Methionine 6. Leucine
2. Threonine 7. Phenylalanine
3. Lysine 8. Tryptophan
4. Valine 9. Histidine
5. Isoleucine 10. Arginine
B. NON-ESSENTIAL / DISPENSABLE AMINO ACIDS
Those which can be produced in the body
Examples:
1. Glycine 7. Glutamic acid
2. Alanine 8. Hydroxyglutamic acid
3. Serinatackse 9. Aspartic acid
4. Norleucine 10. Citruline
5. Tyrosine 11. Proline
6. Cysteine 12. Hydroxyroline
OTHER USES:
Arginine – essential in spermatogenesis
Glutamic acid – has been widely studied for its effect in raising the general intelligence level of
subnormal patients
- Used for the treatment of psychomotor and petit mal attacks
MCP