PROTEINS

Proteins are complex biomolecules that contain

amino acids linked through peptide bonds.

Molecular weight : 6,000 to over 1,000,000

Considered as the most versatile biomolecules
Serve numerous essential functions in biological processes
Primary constituents of living organisms
Contain NITROGEN (N) aside from C, H and O
Foods rich in proteins: animal meat, tuna, cheese, tofu, beans
Proteins are complex biomolecules that contain
amino acids linked through peptide bonds.

 derived from the Greek word “Proteios” – of first importance

 Two Major Types of Proteins:
1) Fibrous proteins (collagen, actin, keratin)
- insoluble in water; main components of the body
2) Globular proteins (albumin, hemoglobin, and
immunoglobulins)
- soluble in water; used for the other non-structural
purposes of proteins.
Proteins play a wide variety of functional roles.

STRUCTURE: form the scaffolding that gives animal cells their

shape. (skin, bones, hair, nails); Collagen & Keratin

HORMONES: Insulin helps cells absorb glucose from the blood &
helps the body from using fat as a source of energy

TRANSPORT: Hemoglobin; involve in the transport of molecules

across cell membranes
 Proteins play a wide variety of functional roles.

 STORAGE: Casein (milk) stores

nutrients for newborn mammals
Ferritin, blood cell protein in the liver,
stores iron

 CATALYST: Enzymes (protein that

speeds up all the reaction
that take place in organisms)

 PROTECTION: antibodies to
counteract & fight disease ;
Fibrinogen = facilitates blood clotting
 Proteins play a wide variety of functional roles.

 MOVEMENT: protein in muscles (myosin & actin) – muscle

contraction and relaxation

REGULATION: control & regulate the kind of protein synthesized

in a particular cell but also dictate the time this
should occur
Amino acids are the building blocks of protein.

Composition: Central C bonded to H, a

carboxyl group (-COOH), an amino
group (-NH2) and a side chain (R
group)
Total amino acids: 20
The R group is the one that is variable
among the 20 amino acids.
 THE TWENTY AMINO ACIDS
(*essential cannot be produced by the body)
Source: http://www.imgt.org/IMGTeducation/Aide-memoire/_UK/aminoacids/formuleAA/#formula

Amino Acid Abbreviations Side chain/R group Linear Formula

Alanine Ala A CH3-CH(NH2)-

COOH

*Arginine Arg R HN=C(NH2)-NH-

(essential amino
acid)
(CH2)3-CH(NH2)-
COOH
*Asparagine Asn N H2N-CO-CH2-
(essential amino
acid)
CH(NH2)-COOH
THE TWENTY AMINO ACIDS
Source: http://www.imgt.org/IMGTeducation/Aide-memoire/_UK/aminoacids/formuleAA/#formula

Amino Acid Abbreviations Side chain/R group Linear Formula

Aspartic Asp D HOOC-CH2-

acid CH(NH2)-COOH

Cysteine Cys C HS-CH2-CH(NH2)-

COOH

Glutamine Gln Q H2N-CO-(CH2)2-

CH(NH2)-COOH
 THE TWENTY AMINO ACIDS
Source: http://www.imgt.org/IMGTeducation/Aide-memoire/_UK/aminoacids/formuleAA/#formula

Amino Acid Abbreviations Side chain/R group Linear Formula

Glutamic Glu E HOOC-(CH2)2-

acid CH(NH2)-COOH

Glycine Gly G NH2-CH2-COOH

*Histidine His H NH-CH=N-CH=C-

(essential amino
acid)
CH2-CH(NH2)-
COOH
 THE TWENTY AMINO ACIDS
Source: http://www.imgt.org/IMGTeducation/Aide-memoire/_UK/aminoacids/formuleAA/#formula

Amino Acid Abbreviations Side chain/R group Linear Formula

*Isoleucine Ile I CH3-CH2-CH(CH3)-

(essential amino acid)
CH(NH2)-COOH

*Leucine Leu L (CH3)2-CH-CH2-

(essential amino acid)
CH(NH2)-COOH

*Lysine Lys K H2N-(CH2)4-

(essential amino acid)
CH(NH2)-COOH
 THE TWENTY AMINO ACIDS
Source: http://www.imgt.org/IMGTeducation/Aide-memoire/_UK/aminoacids/formuleAA/#formula

Amino Acid Abbreviations Side chain/R group Linear Formula

*Methionine Met M CH3-S-(CH2)2-

(essential amino acid) CH(NH2)-COOH

*Phenylalanine Phe F Ph-CH2-CH(NH2)-

(essential amino COOH
acid)

Proline Pro P NH-(CH2)3-CH-

COOH
THE TWENTY AMINO ACIDS
Source: http://www.imgt.org/IMGTeducation/Aide-memoire/_UK/aminoacids/formuleAA/#formula

Amino Acid Abbreviations Side chain/R group Linear Formula

Serine Ser S HO-CH2-CH(NH2)-

COOH

*Threonine Thr T CH3-CH(OH)-CH(NH2)-

(essential amino acid) COOH

Tyrptophan Trp W Ph-NH-CH=C-CH2-

(essential amino CH(NH2)-COOH
acid)
THE TWENTY AMINO ACIDS
Source: http://www.imgt.org/IMGTeducation/Aide-memoire/_UK/aminoacids/formuleAA/#formula

Amino Acid Abbreviations Side chain/R group Linear Formula

Tyrosine Tyr Y HO-Ph-CH2-

CH(NH2)-COOH

*Valine Val V (CH3)2-CH-CH(NH2)-

(essential amino COOH
acid)
Proteins have four levels of structure.

Depends on the
sequence of
the amino acids
According to
complexity:
Primary,
Secondary,
Tertiary &
Quarternary
Proteins have four levels of structure.
Proteins have four levels of structure.

PRIMARY Structure
Linear sequence of amino
acids
Refers to the arrangement
or order of amino acids in
the protein chain
Proteins have four levels of structure.

DIPEPTIDE
 Formed when two amino acids combine through a
condensation reaction
Proteins have four levels of structure.

SECONDARY Structure
Refers to the spatial
arrangement of the
polypeptide chain of a
protein
2 types: Alpha Helix &
Beta Pleated Sheets
 Proteins have four levels of structure.

SECONDARY Structure
Alpha Helix = held
together by H bonds
between loops of a coil
Beta Pleated Sheets =
chains held together by
H bonds between
adjacent chains
Proteins have four levels of structure.

TERTIARY Structure
Refers to the FINAL three-
dimensional shape of a
single polypeptide
molecule where the alpha
helix and the pleated
sheet are folded forming a
GLOBULAR PROTEIN.
Proteins have four levels of structure.

TERTIARY Structure
Types of INTERmolecular
bonds: H-bond, Dipole-
dipole, and London
dispersion
Types of INTRAmolecular
bonds: ionic & covalent
(disulphide bond)
Proteins have four levels of structure.

QUARTERNARY Structure
 Contains more than one
chain
 Refers to the overall shape
when 2 or more
polypeptides bind each
other
 Results in the classification of
proteins: fibrous, globular, or
conjugated
Ex: Hemoglobin
Proteins denaturation involves the disruption and possible
destruction of the secondary and tertiary structures of
protein.
Proteins denaturation can be caused by several factors.

pH changes – alter the IM;

some functional groups of
amino acids lose or gain
electrostatic charge which
affects the formation of
bonds
Increase in Temperature –
disrupt H bonds &
nonpolar hydrophobic
interactions
Proteins denaturation can be caused by several factors.

Addition of various
chemicals – destroy the
natural structure of a
protein
Ex. Addition of Urea (forms
H bonds with different
parts of the protein s
such as peptide groups
causing the weakening
of IMF)
 PROTEINS

Structural Levels:
are made up of Primary May be denatured through:
AMINO ACIDS Secondary pH changes
Tertiary Temperature changes
Quarternary Addition of Chemicals