PROTEINS

Justine Arla Gustilo, RMT

Definition / Description
• Structure:
• polymers of at least 40 amino acid
residues.
• Nutrition:
• provide sulfur and nitrogen to the diet.
• Abundance:
• most abundant macromolecules in
cells.
Definition / Description
• Etymology:
• Johannes Mulder coined the word
protein derived from the Greek word
“proteus”
of first
importance
AMINO ACIDS
Definition
Amino acids are… NH2
• the repeating units of proteins
• molecules that contain an amino group
and a carboxyl group bonded to the
same carbon atom.
COOH
Names and Abbreviations

The 20
common
amino
acids
 Structure
• Basic Structure of amino acids
where the COOH, NH2 and
α - Carbon
R group are bonded
H
H O
Amino N–C–C Carboxyl
(NH2 ) H OH (COOH)
R
any functional
side chain
group
 Structure
Amino acid structure at physiological pH:
H
H O
Amino N – C – C Carboxyl
(NH3+ ) H - (COO -)
H+ O
R

Zwitterion – has both a positive and

negative charge in the same molecule;
no net charge.
D and L Amino Acids
• Only the L – amino acids are the constituent
of proteins.
Review…
Identify the parts of the amino acid shown below:

Cysteine O
Carboxyl
ll -)
(COO
C–O-
Amino l
(NH3+ ) NH3+ – C – H α - Carbon
l
CH2
l side chain
SH
Review…
Is the amino acid in D or L form?

Cysteine O
Carboxyl
ll -)
(COO
C–O-
Amino l
(NH3 )+ NH 3
+–C–H α - Carbon
l
It’s an L-amino acid CH2
bec. the NH3+ is at l side chain
the left.
SH
Isoelectric pH (pHI)
• the pH at which amino acids are neutral
• there will be equal number of positive and
negative charges.
Names, Abbreviations and pKa Values of the Common Amino Acids
Amino Acid Abbreviation α-COOH α-NH2 RH or RH+
Alanine Ala A 2.34 9.69
Arginine Arg R 2.17 9.04 12.48
Asparagine Asn N 2.02 8.80
Aspartic Acid Asp D 2.09 9.82 3.86
Cysteine Cys C 1.71 10.78 8.33
Glutamic Acid Glu E 2.19 9.67 4.25
Glutamine Gln Q 2.17 9.13
Glycine Gly G 2.34 9.60
Histidine His H 1.82 9.17 6.0
Isoleucine Ile I 2.36 9.68
Leucine Leu L 2.36 9.68
Lysine Lys K 2.18 8.95 10.53
Methionine Met M 2.28 9.21
Phenylalanine Phe F 1.83 9.13
Proline Pro P 1.99 10.6
Serine Ser S 2.21 9.15
Threonine Thr T 2.63 10.43
Trytophan Trp W 2.38 9.39
Tyrosine Tyr Y 2.20 9.11 10.07
Valine Val V 2.32 9.62
Classification
Amino acids may be classified according to:
• Essential or Nonessential
• Acidic or Basic
• Ketogenic, Glucogenic or Mixed
 Essential Non-Essential

• CANNOT be produced • CAN be produced bythe

in the body body
• MUST be obtained in • NO NEED to be
the diet obtained in the diet
 Acidic Basic

• Aspartic Acid • Histidine

• Glutamic Acid • Lysine
• Arginine

Her Leggings Are BASIC

 GLUCOGENIC KETOGENIC

• Histidine • Leucine
• Methionine • Lysine
• Valine

Keto Diet: Lamb, Liver

Glucogenic Diet: Honey, Mango, Vanilla
 MIXED

• Isoleucine
• Threonine
• Tyrosine
• Phenylalanine
Essential Amino Acids
• are amino acids that are not produced by the body
and should be obtained from food sources.
• 9 essential amino acids: “Pvt. Mt. Hill”
Phenylalanine H istidine
Valine I soleucine
Threonine L eucine
L ysine
Methionine
Tryptophan
Non - Essential Amino Acids
• are amino acids that are naturally produced by
the body.
• 11 non-essential amino acids:
Alanine Glutamic Acid
Arginine Glycine
Asparagine Proline
Aspartic Acid Serine
Cysteine Tyrosine
Glutamine
Classification of Amino Acids
• Classify the amino acids according to polarity and
essentiality in the body.

Valine Glutamine Histidine

Essential Non - essential Essential

9 essential amino acids: “Pvt. Mt. Hill”

P henylalanine H istidine
V aline I soleucine
T hreonine L eucine
L ysine
Methionine
T ryptophan
Polypeptide Formation
• Amino acids may be bonded
together to form a polypeptide.
chain of amino acids
bonded together.
• The bond between two amino acids
is called a peptide bond.
 Polypeptide Formation
• follows an amino acid sequence.
amino acids present or order or
bonded together arrangement of the
amino acids

G–A–S amino acid sequence

Could also be
glycine serine written as
alanine Gly – Ala – Ser
Polypeptide Formation
G–A–S

O O
ll O- ll
C – O -
C–O- H2O
l 2H+ l
NH3 + – C – H NH3+ – C – H
l l
H CH3

glycine alanine
 Polypeptide Formation
G–A–S
O
peptide bond O ll
ll O- + C – O -
2H
O C–O- H2O l
ll l NH3+ – C – H
C NH – C – H l
l l CH2
NH3 + – C – H CH3 l
l OH
H alanine
glycine serine
Polypeptide Formation
G–A–S O free α -
ll carboxyl
free α - amino O C–O- group
group ll l
O C NH – C – H
ll l l
C NH – C – H CH2
l l l
NH3 + – C – H CH3 OH
l
alanine serine C – terminal
H
glycine N – terminal
Naming of Polypeptides
• last amino acid / C – terminal :
• retain its amino acid name
• other amino acids:
• ends with –yl

G–A–S glycine glycyl

alanine alanyl
glycine serine
alanine serine serine

Name: Glycyl – Alanyl – Serine

FUNCTIONS
Functions
• Structure
• proteins provide stiffness and rigidity to otherwise fluid
– like biochemical systems.

Collagen is a component of
cartilage and skin Elastin is the component of skin
that gives its elasticity
Functions
• Structure

Keratin gives mechanical strength and protective covering to

hair, fingernails, feathers, hooves etc.
Functions
• Catalysts
• all reactions in living systems are catalyzed by
proteins called Enzymes

Oxidases catalyze
Digestive Enzymes oxidation reactions
Functions
• Defense
• proteins are central to the functioning of the body’s
immune system.
Immunoglobulins or
antibodies bind to
foreign substances
such as bacteria or
virus, to help
combat invasion of
the body by foreign
substances

http://www.youtube.com/watch?v=lrYlZJiuf18
Functions
• Messenger
• Hormones transmit signals to coordinate
biochemical processes between different cells,
tissues, organs.
Functions
• Transport
• proteins bind to particular small biomolecules and
transports them to other locations in the body and
then release the small molecules as needed at the
destination.

Hemoglobin carries
oxygen from the
lungs to other
organs and tissues.
 Functions
 Transport

When RBC delivers O2

color changes from red to
purple

When RBC absorbs O2

color changes from blue
purple to red

RBC contains hemoglobin.

Hemoglobin contains “heme”, an
iron containing group which binds to
oxygen.
Functions
• Transport
Transferrin carries
iron from the liver
to the bone
marrow.
Functions
• Storage
• Proteins bind and store small molecules for future use.

MYOGLOBIN
Functions
• Storage

Ferritin

http://www.youtube.com/watch?v=NvNINrtE39g
Functions
• Regulatory
Functions

Myosin
• Movement and
Actin
Functions
• Nutrient

Ovalbumin found in egg white

and provides nourishment for
the developing chick.

Casein found in milk to nourish and

provide immunological protection
for mammalian young.