Introduction to Proteins and amino acid

chemistry
Dr. Dalia Mahmoud Dr. Amal Darwish
Lecturers of Medical Biochemistry and Molecular Biology

12/02/2023
Extended Modular Program 1
 Proteins

Proteins are organic

nitrogenous compounds

Proteins are polymers of α

amino acids monomers
linked together by peptide
bonds

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 Amino Acids
Amino Acids are the Building Blocks of
Proteins

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 Amino Acids structure

• Each amino has an α carbon

atom
• α carbon atom is
asymmetrical (it binds with
different 4 chemical groups or
atoms)
1. Amino group (NH3)
2. Carboxylic group (COOH)
3. H atom
4. R group (variable group or
side chain)

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 Amino Acids structure

• There are 20 amino acids

that enter in the structure of
proteins
• These amino acids differ
from each other in the
structure of their side chains
(R group).
• Amino acids are classified
according to their biological
importance into essential
and non essential amino
acids
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 A- Essential amino acids (10)

• They cannot be synthesized in the body

• Must be taken in food
• They are essential for protein biosynthesis
• They are essential to normal health
• Deficiency leads to disease
• Essential amino acids are 10 in number abbreviated as PVT TIM
HALL
Phenylalanine, Valine,Threonine,Tryptophan, Isoleucine,
Methionine, Histidine, Arginine, Leucine, Lysine
 B. Non essential amino acids

• They can be synthesized inside our body

• Important for protein synthesis
• They are the other 10 amino acids
 Peptide bond Formation
• Proteins are made of many -amino acids linked together
by peptide linkages (bonds).
• Peptide bonds are covalent bonds

8
 Peptide bond breakage

Inside
Outside body
body

Strong acid Peptidase

High
(proteolytic)
or base Temperature Enzyme
9
Bonds responsible for protein structure
and stability

SHARING IS
CARING!
Bonds

Non
Covalent
covalent

Electrostatic Hydrophobic
Peptide Disulfide Hydrogen interaction interaction
 Covalent bonds
1. Peptide bond
2. Disulfide bond (-S-S-)
– It occurs between 2 cysteine
amino acids
 Non covalent bonds
1. Hydrogen bonds:
• They are weak in comparison to
covalent bonds

• But because of their large number in

proteins they collectively responsible
for protein stability
 Non covalent bonds
2. Electrostatic interaction (ionic bond)
– Attraction or repulsion between charged
groups of protein
 Non covalent bonds
3. Hydrophobic interaction:
• Amino acids with nonpolar side chains tend to be located in the
interior of the polypeptide chain ,
• In contrast, amino acids with polar or charged side chains tend to
be located on the surface of the molecule in contact with the
polar solvent.
Levels of protein structure

Primary

Secondary

Tertiary

Quaternary
 Primary structure of proteins
• Refers to sequences of amino acids in the polypeptide
chain, linked by peptide bonds.
• Each protein has specific number, specific types and
specific sequences of amino acids
 Secondary protein structure
• It is the local folding of the polypeptide chain to form
certain regular confirmations
• These regular forms of secondary structure include:
1. α- helix
2. β- pleated sheets
• These forms are kept stabilized by interactions of by
hydrogen bonds
α- Helix - pleated sheet
 Tertiary structure of proteins
• It is the three dimensional structure of proteins
(protein folding)

• Bonds of tertiary structure

– Disulfide bonds (covalent bond)
 Hydrogen bonds (non covalent)
 Hydrophobic interactions (non covalent)
 Electrostatic interactions (non covalent)
 Quaternary structure of proteins
• A protein that contains 2 or more polypeptide chains held
together by non covalent bonds is said to have quaternary
structure
• The individual polypeptide chain (subunit) is termed
monomers
• The subunits may or may not be identical
• Examples:
– Hemoglobin : contains 4 polypeptide chain
The four levels of protein structure
 Daily recommended requirement of
proteins

The recommended daily

This amount increases
requirement for protein
in child and in pregnant
for an adult is about 0.8
or lactating female.
grams protein /Kg.

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 A. Classification of proteins according to
function
Transport : hemoglobin

Regulatory: hormones,
insulin

Catalytic: enzymes

Defense function:
immunoglobulins

In cell membrane
structure

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 B. Protein classification According
to the biological value
High biological value Low biological value
proteins proteins
• Contain all essential • Lack one or more
amino acids required essential amino acids
for synthesis of human
tissue proteins.
• Proteins of animal
origin: meat liver, milk,
fish
• Some plant proteins
(beans, lentils) in
combination
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 Protein classification According to the
biological value

High biological value Low biological value

proteins proteins

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 C. Classification of proteins According to
the shape
A. Fibrous proteins:
• e.g. Collagens, elastin and laminin
• They the principal structural proteins of the connective
tissues
B- Globular proteins :
e.g. Hemoglobin and myoglobin
Examples of fibrous and globular
proteins
 Collagen
• Collagen is the most abundant protein in the human body
• It represents the major component of bones, tendons, ligaments,
teeth (dentin of the teeth), blood vessels and skin .
• It is formed of three polypeptide chains (α chain) which are wound
around each other in a rope-like triple helix ( tropocollagen)
 Keratins
• It is the major components of hair, nails
and outer layers of the skin
• It is rich in cystein which form disulfide
bonds
 Protein digestion
• Dietary proteins must be digested into amino acids and small
peptides.
• As the dietary proteins are not absorbed.
• No single enzyme can digest protein (many enzymes are
secreted from stomach, pancreas and small intestine for the
digestion of proteins)
Protein digestion
 Digestion of protein by digestive enzyme in
the stomach

Protein digestion Pepsin enzyme is Pepsinogen is

starts in the stomach secreted from activated by the
through secretion of stomach cells as an
an enzyme called inactive form (called acidity (HCL) of the
pepsin. pepsinogen). stomach.
 Digestion of protein by digestive enzymes
from pancreas

The pancreatic
When the stomach proteases (proteases=
Pancreatic digestive enzymes that digest
empties its content into
small intestine , the enzymes also, are proteins) are trypsin,
pancreas will secrets secreted as an chemotrypsin,
its digestive enzymes. inactive form. elastase,
carboxypeptidases.
 Digestion of protein by enzymes from intestinal
cells

Aminopeptidases are Aminopeptidases

secreted from the release one amino
intestinal cells. acid from the peptide.

Now amino acids are ready to be absorbed by intestinal cells.

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