PROTEIN

Mark Raymund G. Nava, RMT, MPA, MSMT

Assistant Professor
 PROTEIN
naturally occurring, unbranched polymer
in which the monomer units are amino
acids
peptide in which at least 40 amino acid
residues are present
also known as polypeptide
 FUNCTIONS
contain Carbon, Hydrogen, Oxygen,
Nitrogen, sometimes Sulfur and
Phosphorous
serve as structural components of
animals
serve as control molecules (enzymes)
serve as transport and messenger
molecules
 AMINO ACIDS
Building blocks of proteins
Organic compound that contains both an
amino group and a carboxyl group
700 different naturally occurring amino
acids but only 20 are normally present in
proteins Standard Amino Acids
AMINO ACIDS
 AMINO ACIDS
Amino group acts like a base, tends to be
positive
Carboxyl group acts like an acid, tends to
be negative
R group is variable, from 1 atom to 20
two amino acids join together to form a
dipeptide
adjacent Carboxyl and Amino groups bond
together
SOME AMINO ACIDS
SOME AMINO ACIDS
SOME AMINO ACIDS
 CLASSIFICATION
base on side chain polarity
Classification Description
1 amino group
Non- Polar 1 carboxyl group
Amino Acids 1 non polar side chain
1 amino group
Polar Neutral 1 carboxyl group
Amino Acids 1 polar neutral side chain
1 amino group
Polar Acidic 2 carboxyl group
Amino Acids (1 is part of side chain)
2 amino group
Polar Basic (1 is part of side chain)
Amino Acids 1 carboxyl group
 CLASSIFICATION
base on side chain polarity
NON-POLAR AMINO ACIDS
POLAR AMINO
Glycine Gly G
Alanine Ala A
ACIDS
Valine Val V Serine Ser S
Leucine Leu L Cysteine Cys C
Isoleucine Ile I Threonine Thr T
Proline Pro P Asparagine Asn N
Phenylalanine Phe F
Glutamine Gln Q
Methionine Met M
Tyrosine Tyr Y
Tryphtopan Trp W
 CLASSIFICATION
base on side chain polarity
POLAR ACIDIC AMINO POLAR BASIC AMINO
ACIDS ACIDS
Aspartic Histidine His H
Asp D
Acid
Lysine Lys H
Glutamic
Glu E Arginine Arg R
Acid
ESSENTIAL AMINO ACIDS
Arginine Methionine
Histidine Phenylalanine
Isoleucine Threonine
Leucine Tryptophan
Lysine Valine
 CHIRALITY OF AMINO ACIDS
All 20 standard amino acids have chiral
centers except GLYCINE
Hence, amino acids have mirror images:
Right and Left based on the location of the
amino group
Nature favors/prefers the L-isomers of
amino acids
CHIRALITY OF AMINO ACIDS

COOH

H2N C H

R
ACID-BASE PROPERTIES
OF AMINO ACIDS
H

H2N C COOH

R
 ACID-BASE PROPERTIES
OF AMINO ACIDS
Both acidic and basic group are present in
an -amino acid
In solution, three different amino acids
exist: a zwitterion, a negative ion and a
positive ion
If in crystal form, not soluble with water
due to strong intermolecular forces
 ISOELECTRIC POINT
The pH at which an amino acid has no net
charge because equal number of positive
and negative charges are present
Example:
alanine - 6.01
glycine - 5.97
valine - 5.97
Formation of a Dipeptide

Dehydration synthesis
 Amino Acid + Amino Acid Dipeptide

Amino Acid + Dipeptide Tripeptide

A.A. + A.A. + ..+ Tripeptide Polypeptide
 Naming Peptides
IUPAC Rules in naming small peptides

RULE 1:
The C-terminal amino acid residue keeps
its full amino acid name
 Naming Peptides
IUPAC Rules in naming small peptides
RULE 2:
All the other amino acid residue names
ending in -ine or ic acid will be
replaced with yl, except:
Tryphtopan Tryptophyl; Cysteine Cysteinyl;
Glutamine Glutaminyl; Asparagine - Asparaginyl
 Naming Peptides
IUPAC Rules in naming small peptides

RULE 3:
The amino acid naming sequence begins
at the N-terminal amino acid residue
 Naming Peptides
IUPAC Rules in naming small peptides

EXAMPLE:
Glu Ser Ala

glutamyl seryl alanine

Glutamylserylalanine
 CLASSIFICATION OF PROTEIN
base on number of peptide chain
1. MONOMERIC only one peptide chain
is present

2. MULTIMERIC more than one peptide

chain is present
 CLASSIFICATION OF PROTEIN
base on chemical composition
1. SIMPLE only amino acid residues are
present

2. CONJUGATED one or more non-amino

acid entities present in its structure in
addition to one or more peptide chains
 Conjugated Proteins
Simple Prosthetic Conjugated
Protein + Group
= Protein

Peptide Organic or
chain Inorganic
non-amino acid
component
 Conjugated Proteins
CLASS PROSTHETIC GROUP EXAMPLE
Hemoglobin
Hemoproteins Heme unit Myoglobin
LDL, HDL, VLDL and
Lipoproteins Lipids Chylomicrons
Gamma Globulin
Glycoproteins Carbohydrate Mucin
Interferon
Phosphoproteins Phosphate group Glycogen phosphorylase
Ribosomes
Nucleoproteins Nucleic Acids Viruses
Ferritin
Metalloproteins Metal Ion Alcohol Dehydrogenase
STRUCTURE OF PROTEIN
Alpha Helix
Beta Pleated Sheets
 CLASSIFICATION OF PROTEIN
base on shape
1. FIBROUS have an elongated shape
with one dimension much longer than
the others

2. GLOBULAR have peptide chains folded

into spherical and globular shapes
Fibrous Versus Globular Proteins
FIBROUS GLOBULAR
Extended protein Compact protein
structure structure
Insoluble in water Soluble in water
Secondary structure is
Secondary structure is complex mixture of
simple -helix, -sheet, loop
structures
Functions for support
Functions in all aspects
and external
of metabolism
protection
Fibrous Versus Globular Proteins
 PROTEIN HYDROLYSIS
splits peptide bonds to smaller peptides and
amino acids
occurs in the digestion of proteins
occurs in cells when amino acids are needed
to synthesize new proteins and repair tissues
In the lab, hydrolysis of a peptide requires acid
or base, water, and heat
In the body, enzymes catalyze the hydrolysis of
proteins
Hydrolysis of Peptide

H2O enzymes
 DENATURATION
involves the disruption of bonds in the
secondary, tertiary, and quaternary structures
heat and organic compounds break apart H
bonds and disrupt hydrophobic interactions
acids and bases break H bonds between
polar R groups and disrupt ionic bonds
heavy metal ions react with SS bonds to
form solids
agitation (whipping, shaking) stretches
peptide chains until bonds break

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 Applications of Denaturation
Cooking eggs
Wiping of alcohol
Heat used to cauterize
blood vessels
Sterilization of
instruments in
autoclave
Hair perming

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