CHAPTER 4 Protein and Amino Acid

Chemistry
LEARNING TARGETS:
At the end of the lesson, the students can:
 Enumerate the general characteristics of proteins.
 Diagram the general structure of amino add.
 Describe the physical properties of amino acids.
 identify and characterize the different classification of amino acids.

What are PROTEINS?

An extraordinary number of different proteins, each with a different
function, exist in the human body. A typical human cell contains about 9,000
different kinds of proteins, and the human body contains about 100,000 different
proteins. Proteins are important for the synthesis of enzymes, certain hormones,
and some blood component; for the maintenance and repair of existing tissues;
for the synthesis of new tissue, and sometimes for energy.

GENERAL CHARACTERISTICS OF PROTEINS

Proteins are the most abundant substances in nearly all cells next to water. They account for about
15% of cell’s overall mass. All protein contains the elements carbon, hydrogen, oxygen, and nitrogen.
The presence of nitrogen in proteins set them apart from carbohydrates and lipids, which most often
do not contain nitrogen. Other elements such as sulfur, phosphorus, and iron are essential
constituents of certain specialized proteins.
Casein, the main protein of milk, contains phosphorus, an element which is very important in the
diet of infants and children. Hemoglobin, the oxygen-transporting protein of blood, contains iron.

AMINO ACIDS: THE BUILDING BLOCKS OF PROTEINS

An amino acid is an organic compound that contains both an amino (-NH 2)
group and a carboxyl (-COOH) group. The amino acids found in proteins are
always alpha-amino acids. An alpha-amino acid is an amino acid in which the
amino group and the carboxyl group are attached to the alpha carbon atom. As
with carbohydrates, it is traditional to use the D and L nomenclature with amino
acids based on the configuration of glyceraldehyde.
The structure of an alpha amino
acid in its un-ionized form

CHO CO2H

L - glyceraldehyde L - alanine
Naturally occurring amino acids generally have the same configuration as L – glyceraldehyde
configuration at the alpha-carbon.

GENERAL STRUCTURE OF AMINO ACIDS

The general formula for alpha-amino acid is shown below:

R<--- side chain

Amino group NH 2 — C — COOH carboxyl group

H alpha carbon atom

It is called an alpha-amino add because both amino and carboxyl groups are attached to the alpha carbon
atom. All of the 20 amino adds found in proteins have a common denominator: a carbon and an amino
group bonded to the same carbon atom. The amino acids differ from each other in their side chains, or R
groups, which vary in structure, size, electric charge, and solubility in water.

Examination of the above formula discloses the fact that

the alpha carbon atoms have 4 different groups attached
to it (except for the case where R is H like glycine), so this
carbon is asymmetric, and because of the presence of this
asymmetric carbon atom, amino acids are capable of optical
rotation, except glycine, because the phenomena of optical
rotation is due to asymmetry.

Amino acids are optically active molecules and

asymmetry of their mirror images is not superimposable (except
in the case of glycine where the R-group is hydrogen).

GENERAL CHARACTERISTICS OF AMINO ACIDS

Amino acids are colorless crystalline substances soluble in water and insoluble in organic solvents with a
high melting point.
Various ways of classifying the amino acids on the basis of their R groups have been proposed. The most
meaningful is based on their polarity, i.e., their tendency to interact with water at biological pH (near pH
7.0). There are 5 main families of amino acids based on the polarity of their R-groups or side chains.
Amino acids are classified on the basis of the structure of R.

1. Aliphatic side chains – hydrophobic

ALIPHATIC SIDE CHAINS – HYDROPHOBIC

2. Polar side chains - text classifies as HO-, S-, and amide containing - hydrophilic

POLAR SIDE CHAINS HYDROPHILIC

3. Acidic – hydrophilic

ACIDIC – HYDROPHILIC

4. Basic – hydrophilic
 BASIC – HYDROPHILIC

5. Heterocyclic/Aromatic —hydrophilic or hydrophobic

Heterocyclic/Aromatic

ANOTHER WAYOF CLASSIFYING AMINO ACIDS

A. Neutral amino acids- they are monoamine-monocarboxylic (with one as well as other
substituents distinguish these amino acids from each other).
1. Straight-chain
a.Glycine
b.Alanine
c.Serine
 d.Threonine
2. Branched-chain amino acids
a.Valine
b.Leucine
c . Isoleucine

B. Aromatic amino acids- these consists of amino acids with phenyl hydroxyphenyl, or indole
rings substituted on alanine.

1. Phenylalanine- contains the phenyl ring

2. Tyrosin- contains the hydroxyphenyl ring
3. Tryptophan- contains the indole ring

C. Essentials and Non-essentials amino acids

1. Cysteine
2. Homocysteine
3. M e t h i o n i n e

D. Basic amino acid

1.Lysine
2. Ar g inine
3. Hist id ine

E. Acidic amino acids

1. Aspartic acid
2. Glutamic acid

F. Amino acids - a molecule that contains both imine (>C=NH) and carboxyl (-C(=0)-0H)
functional groups.
1. Proline
2. Hydroxyproline

PHYSICAL PROPERTIES OF AMINO ACIDS

1. Solubility - amino acids exhibit a wide range of solubilities. In general , amino acids are
minimally soluble at their isoelectric points. Those amino acids with longer aliphatic side
chains are less soluble (e.g., leu, lie, Val) than those with shorter chains (e.g., Gly, Ala.) polar
groups such as carboxyl and hydroxyl, tend increase solubility.
2. Melting point - amino acids possess' high melting points, usually above 200°C.
3. Tastes of amino acids - amino acids are usually sweet, tasteless, or bitter. Glycine, alanine,
valine, and serine are sweet. Leucine is tasteless; isoleucine is bitter.
4. Appearance - the amino acids are white crystalline substance; the crystal from being
characteristic for each one.
5. Ultraviolet absorption spectrum of aromatic amino acids - the aromatic amino acids
tryptophan, tyrosine, and phenylalanine absorb ultraviolet light. Most of the UV absorption of
proteins is due to their tryptophan content.
6. Optical properties of amino acids - the alpha carbon atoms of all the amino acids except
glycine are asymmetric, so they show optical activity. The rotations of the amino acids vary
according to the pH of the solution, which determines the ionic state of the amino acid.
7. Acid-base properties of amino acids- amino acids in aqueous solution are ionized and
can act as acids or bases. Those amino acids having a single amino group and a single carboxyl
group crystallize from neutral aqueous solutions in a fully ionized species called dipolar ion or
zwitterion. These dipolar and negative charges. Below is the formula of zwitterion:

NH3+

R C COO

H
Zwitterion