Protein

By El Wathan
Organic Chemistry for third grade
Out Line

Definition Structures Bonds Classifications

1 2 3 4

Functions Sources Analysis

5 6 7
 Definition

#aminoacid #Peptidebond #peptides

#polypeptides
Definition

are macromolecules
that consist of one or
Proteins
more polypeptide chains
Definition

are polymer chain of

amino acid as monomer
Polypeptide
linked by peptide bonds
Definition

are bi-functional
compounds that contain
Amino Acid amine and carboxylic
acid which are attached
to α carbon
Definition

are a covalent bond in

amide functional group
Peptide Bond that are formed from
reaction between two
amino acids
 Structures

#primary #secondary #tertiary

#quarternary #folding
Structures

Primary Secondary
Protein Protein

Tertiary Quarternary
Protein Protein
Structures

im ar y Linear structure of protein and there is no interaction

Pr beside peptide bond between amino acid
Protein
Structures
2 regular
folding
patterns have
been
identified –
formed
between the
bonds of the
peptide
backbone

o nd ary Regular folding of polypeptide chain as a result of

S e c hydrogen interaction between every amino acid
Protein
Structures
2 regular
folding
patterns have
been
identified –
formed
between the
bonds of the
peptide
backbone

o nd ary Regular folding of polypeptide chain as a result of

S e c hydrogen interaction between every amino acid
Protein
Structures
2 regular
folding
patterns have
been
identified –
formed
between the
bonds of the
peptide
backbone

o nd ary Regular folding of polypeptide chain as a result of

S e c hydrogen interaction between every amino acid
Protein
Structures
2 regular
folding
patterns have
been
identified –
formed
between the
bonds of the
peptide
backbone

o nd ary Regular folding of polypeptide chain as a result of

S e c hydrogen interaction between every amino acid
Protein
Structures Core of many proteins is
the -sheet
Form rigid structures with
the Hydrogen bond
Can be of 2 types :
-sheet Anti-parallel – run in an
opposite direction of its
neighbor (A)

Parallel – run in the same

direction with longer

o nd ary looping sections between

S e c them (B)

Protein
Structures Formed by a Hydrogen bond
between every 4th peptide
bond – C=O to N-H

Usually in proteins that span a

membrane

α-helix
The  helix can either coil to
the right or the left

Can also coil around each

o nd ary other – coiled-coil shape – a

S e c framework for structural
proteins such as nails and skin
Protein
Structures

T ert ir ay Irregular folding of one polypeptide chain as a result of

many interactions between side group in every different
Protein amino acid
Structures

T ert ir ay Irregular folding of one polypeptide chain as a result of

many interactions between side group in every different
Protein amino acid
Structures

t e r na ry
Qua r Irregular folding of two or more polypeptide chains as
a result of many interactions between side group in
Protein every different amino acid
Structures
 Bonds

#peptidebond #hydrogenbond #saltbridge

#disulfidebridge #vanderwaalsinteraction
#hydrophobicinteraction
Bonds Peptide Bond
Bonds Peptide Bond
Bonds Hydrogen Bond
Bonds Salt Bridge
Bonds Disulfide Bridge
Bonds Disulfide Bridge
Bonds Van Der Waals Interaction
Bonds Hydrophobic Interaction
Bonds
Classifications

#globular #fibrouos #simple

#conjugated #derived
Classification
base on Shape
Extended protein structure

F ibrous Insoluble in water (or in lipid bilayer)

Secondary structure is simple based on one type only

Quarternary structure is usually held together by covalent

Functions in structure of the boady or cell (tendons, bones, mudcle, ligaments, hair, skin)
Classification Examples
base on Shape Elastin

F ibrous
Classification Stabilizing Cross-Links
Examples
base on Shape • Cross linkages can be between 2 parts of a Elastin
protein or between 2 subunits

F ibrous
• Disulfide bonds (S-S) form between adjacent
-SH groups on the amino acid cysteine
Classification Examples
base on Shape Keratin

F ibrous
Classification
base on Shape
Compact protein structure

G lobular Soluble in water (or in lipid bilayer)

Secondary structure is complex with mixture of α-helix, -sheet, and loop structures

Quarternary structure is held together by non covalent forces bridges

Functions in all aspects of metabolism (enzymes, hormones, ect.)

Classification Examples
base on Shape Hemoglobin

Globular
Classification Examples
base on Shape Globulin

Globular
Globulin

Is a generic term used to describe a set of sixty proteins including antibodies or gamma
globulins
Classification
base on Composition

Simple
Protein that contain
Histone
only amino acid as Example
Protamine
composition
Classification Examples
base on Composition Histone

Simple
Classification
base on Composition

Conjugated
Lipoprotein
Protein that contain not Glycoprotein
only amino acid as Example Nucleoprotein
composition Metaloprotein
Chromoprotein
Classification
base on Composition

Conjugated
Lipoprotein
Protein that
has LIPIDS
as prosthetic
group
Ex. Peripheral
apoprotein
Classification
base on Composition

Conjugated

Glycoprotein
Protein that has
CARBOHYDRATE
as prosthetic group
Ex. Some membrane
Classification
base on Composition

Conjugated
Nucleoprotein
Protein that has
DNA/RNA as
prosthetic group
Ex. Nucleosome
Classification
base on Composition

Conjugated
Metaloprotein
Protein that
has METAL
as prosthetic
group
Ex. Hemoglobin
Classification
base on Composition

Conjugated
Chromoprotein
Protein that has
CHROMOPHORE
group as prosthetic
group
Ex. Myoglobin
Classification
base on Composition

Derived
Protein that has been
Coagulated Casein
modified by chemicals, Example
Denatured Protein
heats, or enzymes.
 Functions

#structural #functional #enzyme

#hormone #transport #storage
Functions Structural
One of the important function of protein is structural,
ex. Collagen (A) and Elastin (B)
 Functions Functional

Enzymes
Hormones
Antibodies
Storages
Transport
Enzymes are proteins that bind to their ligand as the 1 st step in a process

An enzyme’s ligand is called a substrate

May be 1 or more molecules

Output of the reaction is called the product

Enzymes can repeat these steps many times and rapidly, called catalysts

Example is Trypsin
 Functions Functional
Ligan Binding
Enzymes
Hormones
Antibodies
Storages
Transport
 Functions Functional
Ligan Binding
Enzymes
Hormones
Antibodies
Storages
Transport
 Functions Functional

Enzymes
Hormones
Antibodies Ex. insulin
Storages Protein can be used to deliver chemical
Transport information needed in metabolism inside
Ex.
Ex. Adrenalin
Oxytocin
the body
 Functions Functional

Enzymes
Hormones
Antibodies
Storages
Transport
A family of proteins that can be created to bind to
almost any molecule

Antibodies (immunoglobulins) are made in response to a

foreign molecule ex. bacteria, virus, etc. called the antigen

Bind together tightly and therefore inactivates the

antigen or marks it for destruction
 Functions Functional

Enzymes
Hormones
Antibodies
Storages
Transport
 Functions Functional

Enzymes
Hormones
Antibodies
Storages
Transport
Y-shaped molecules with 2 binding sites at the
upper ends of the Y

The loops of polypeptides on the end of the binding

site are what imparts the recognition of the antigen

Changes in the sequence of the loops make the

antibody recognize different antigens - specificity
 Functions Functional

Enzymes
Hormones
Antibodies
Storages Ex. Albumin
Protein can be used to store a specific
Transport molecule and release the molecule when it
Ex. Wheyisprotein
needed
 Functions Functional Example is
Hemoglobin
can transport
Enzymes Oxygen
Hormones
Antibodies
Storages
Transport
Protein can be
used to
transport a
specific
molecule
inside the
body.
 Sources

#eggs #soy #milk

Sources

Casein

Milk
Sources

Soy Protein

soy
Sources

Albumin

Egg
 Analysis

#qualitative #quantitative #biurettest #electrophoresis

#kjeldahlmethod #nitrogencontain
Analysis

Biuret Test

Identification Using CuSO4 to

protein by from complex
peptide bond blue solution
Qualitative
Analysis
Analysis

Kjeldahl Method

Determide the Using 3 step :

Destruction (Cons Acid)
amount of Nitrogen Destilation (Strong Base)
atom in protein Titration
Quantitative
Analysis
Thank you

El Wathan