Proteins

19-1
Lecture outline
Biologically important proteins - functions
Hemoglobin, myoglobin, myosin, elastin, keratin, fibrin,
Collagen, insulin, albumin, immunoglobulins, …….

General Properties

Classification according to function, shape, structure and composition.

General composition of proteins

Structure of proteins

Amino Acids and the Peptide bond – property and function

Essential and non-essential amino acids
Diseases related to deficiency of some amino acids
Parkinson’s Disease, Alzheimer, maple syrup urine disease, alkaptonuria, cystinuria, hartnup
disease, homocystinuria, phenylketonuria, ornithine transcarboamylase deficiency

Chemical reactions: Coagulation, Denaturation, Renaturation and precipitation - Practical Application. 19-2
Biological importance
• structural support, biochemical catalysts, hormones, enzymes,
building blocks, and initiators of cellular death.

• help in metabolism by providing structural support and by acting as

enzymes, carriers, or hormones.

19-3
 General properties of proteins:

• “protein” is derived from the Greek word “proteios” meaning of first

importance.
• most important and most abundant of all biological compounds.
• a naturally occurring unbranched polymer in which the monomer units are
amino acids
• About 15% of cell’s overall mass.
• Contains elements of carbon, hydrogen, nitrogen and sulfur
• The presence of nitrogen and sulfur makes protein differs from
carbohydrates and lipids.
General properties of proteins:
• Contains an average of 15.4% by mass of nitrogen

• Phosphorus and iron are essential constituent of certain specialized

protein.

• Casein – main protein in milk contains phosphorus (very important

in the diet of infant and children)

• Hemoglobin : the oxygen – transporting protein of blood.

 General properties of proteins:
• organic compounds of high molecular weight made up
of amino acids joined by means of peptide linkages.
(15,000 to 20,000)
• different types and biological functions of proteins
like:
keratin of skin, hair and fingernails,
insulin that regulates glucose metabolism ,
DNA polymerase that catalyzes the synthesis of
DNA in cells .
Carry out most of the work of the cell
 Proteins: types and
functions:
• are biological catalysts (enzymes)

• are antibodies that fight antigens (bacteria and viruses)

• transport molecules and ions

• regulate cell function

• provide structural support and mechanical strength

• are necessary for all forms of movement

• are sources of amino acids for growth

19-8
PROTEINS
• GENERAL COMPOSITION OF PROTEINS

C= 15% O = 24% N = 16%

S= 1.0% P = 0.4% H = 7%
General formula of protein

α carbon or
chiral carbon
• amino group and the carboxyl group are attached to the  − carbon
atom.
•  − carbon atom has an R group side chain except for glycine which
has two H atoms.
• they are Zwitterions (German word: zwitter – “hybrid”)

H O
Generic amino +
acid at physiological H3N C C O
pH. C R1
 Amino acid: Zwittterion
• Amino acid exist in
zwitterion
✓in water solution and in solid
state
✓differ in physical & chemical
properties
✓ high melting points

• The molecular form does

not exist.
 Amino acid: structure
•If the R group is not H, the amino acid, AA can exist in two
enantiomeric forms (nonsuperimposable mirror image)

O O O O
C C
+ +
H3N C H H C NH3
R1 R1
Mirror plane
Amino acids incorporated into  carbon
proteins have the L- configuration.
 Amino acid structure:
R group side chain

• Distinguishes the difference of the α – amino

acids from each other

• Varies in shape, size, charge, acidity,

functional groups present, hydrogen –
bonding ability and chemical reactivity.
Amino acids
• around 700
different
naturally
occurring amino
acids

• only 20 standard
amino acids :
normally present
in proteins
 Amino acids
Classified as to:

Essential

Non-essential
Amino
acids,
structure
According
to
their
properties
Example in writing amino acids:

α carbon or
chiral carbon

19-18
Amino
acid
structure

According to
their
properties
Aliphatic amino acid structures

19-20
 Side Chains with alcohol groups
Catalytic role: phosphorylation,
o-glycosylation, hydrogen bond

Threonine (Thr, T) have

uncharged polar side chains
 Structures of aspartate,
glutamate ,
R group contains carboxyl group

19-22
Structures of asparagine
and glutamine
R group contains C = O and NH2

19-23
Structures of histidine, lysine
and arginine

19-24
 Structures of methionine
and cysteine
Containing sulfur
Methionine: First aa
Cysteine : Catalytic role,
disulfide bond

19-25
Formation of cystine

19-26
Aromatic amino acid structures

phosphorylation
 Proline structure
• Proline has a nitrogen in the
aliphatic ring system

• Proline has a three-carbon side

chain bonded to α-amino nitrogen

• The heterocyclic pyrrolidine ring

restricts the geometry of
polypeptides

19-28
Aromatic
R groups

19-29
Positively charged R groups

19-30
Negatively charged R groups

19-31
Groups/classes of α-amino acids according to side-chain
polarity
• Nonpolar / hydrophobic (water fearing)

• Polar / hydrophilic (water loving)

Polar neutral amino acids
Polar acidic amino acids / negatively charge amino acid
Polar basic amino acids / positively charge amino acid
Nonpolar, aliphatic R groups

19-33
Polar,
uncharged
R group

19-34
Groups/classes of α-amino
acids according to side-
chain polarity
Nonpolar amino acids
(hydrophobic)

• 1 amino & 1 carbonyl

grp. and 1 nonpolar
side chain

• interior of protein
(buried)

• 9 amino acids
Groups/classes of α-
amino acids according
to side-chain polarity
Polar amino acids
• Polar neutral amino acids

✓1 amino & 1 carbonyl grp. and a

side chain: polar but neutral
✓R group – high affinity for water
✓not ionic (unionic) @ pH 7
✓cysteine molecules form disulfide
bonds with one another
✓6 amino acids
Groups/classes of α-amino
acids according to side-
chain polarity
Polar amino acids
• Polar acidic amino acids (negatively
charge amino acid)
✓1 amino & 2 carbonyl grp. and a side
chain; the 2nd carbonyl grp. is part of a
side chain
✓@ pH 7 : net charge is – 1; side chain
contains negative grp.
✓acidic: ionization of carboxylic acid
releases a proton
✓2 amino acids
Groups/classes of α-amino acids according to
side-chain polarity
Polar amino acids
• Polar basic amino acids (positively
charge amino acid)
✓ 2 amino & 1 carbonyl grp. and a side chain
; the 2nd amino grp. is part of a side chain
✓ @ pH 7 : net charge is + 1 ; side chain
contains positive grp.
✓ basic: side chains reacts with water,
picking up a proton and
release a OH –
✓ 3 amino acids