CREATD BY :

Johandi
Mila karmila wati
Putri maya juvitasari
Santy
Selly marsella
Sugandi

protein
Proteins are complex organic compounds of
high molecular weight, proteins are polymers of
amino acid monomers linked together by
peptide bonds. Protein molecules containing
carbon, hydrogen, oxygen, nitrogen and
sometimes sulfur and phosphorus. Proteins play
an important role in the structure and function
of all living cells and viruses.
The properties of proteins
1. Ionization when the protein soluble in water to form positive
ions negative ions dab.

2. Denaturation which changes the conformation and position
of the protein so that its activity is reduced or the ability to
support the activities of certain organs in the body so that
the body has lost poisoning.

3. Viscosity whereby those incurred by the presence of friction
between the molecules in the liquid flowing.

4. Crystallization is a process that is often done by the addition of
ammonium sulfate salts or NaCl solution with pH adjustment at
the isoelectric point.

5. Colloidal system is a heterogeneous system consisting of two
phases, namely the small particles are dispersed from the
dispersing medium or solvent.

Proteins can consist of one or more polypeptide, for
example myoglobin consist of two polypeptide and
hemoglobin consist of four chain polypeptide
Compound of peptide is result polymerization of acid
Amino. The molecules of amino acid bound each other that
be connected by group amide which called peptide bond
which be formed between NH
2
group of acid amino one
with group COOH of amino acid another.
Structure Peptide and Nomenclature
Peptide is polymerization result of amino acid, so that
structure of peptide consist of two or more Amino acid.
Peptide which consist of two molecule amino acid is called
dipeptide,when consist of 3, 4.5 and 6 of amino acid are
called tripeptide,tentra peptide,penta peptide and hexa
peptide. For peptide which consist of many acid amino is
called polypeptide. In writing structure of peptide, group
NH
2
free (rest NH
2
) always situate in next left which be
called end-N and group COOH free (rest COOH) always
situate in next right which be called end-C.
Amino acid contain end -N is
called N-terminal amino acid
and amino acid contain end
-C is called C-terminal amino
acid.
All of peptide structure often abbreviated with bundle symbol
three letter of abbreviation name amino acid certain which order
appropriate with order amino acid compiler peptide mentioned,
for example dipeptide which form of glycine and alanine
structure, that have two possibility of glycine and alanine structure
namely:
classification of proteins
Based on constituent :
A.Proteins simple
Proteins simple is protein only consist
above molecule acids Amino.
Is a polypeptide
Example: albumin, histones.
B. Protein conjugation
Protein conjugation is a polypeptide
that is bound to nonprotein group
prosthetic group
Example: nucleoprotein, lipoproteins,
and metaloprotein fosfoprotein.
Proteins conjugation classified based
group prosthetic
Based shape:
Proteins fibrous
1. Shaped lengthwise like thread
2. Proteins were there on animal
3. not soluble in water,
4. Provide role structural,
5. Examples : Collagen constitute protein main which form
network bundle.Elastin there in veining,muscle,artery (vessel
blood). Keratin there in hair and nails.
Globular proteins
1. Soluble in water
2. Globular proteins shaped round
3. Form fold (Spherical shape) with section hydrophilic be
surface
4. Function as enzyme,hormone,and transport proteins
5. Examples : Albumin there in eggs,milk, Plasma, and
hemoglobin. Globulin there in muscle, Serum, yellow
eggs.Histon there in networks like thymus and
pancreas. Protamine connected with acid nucleic.


levels of protein structure
There are 4 level of protein structure :
1. The primary structure
sequence of amino acids that form the polypeptide
chain

2. The secondary structure
Secondary structure is a local regulary occuring structure in
proteins and is mainly formed through hydrogen bonds
between backbone atoms. So-called random coils, loops or
turns don't have a stable secondary structure. There are two
types of stable secondary structures: Alpha helices and beta-
sheets . Alpha-helices and beta-sheets are preferably located
at the core of the protein.

3. The tertiary structure
Tertiary structure describes the packing of alpha-helices, beta-
sheets and random coils with respect to each other on the level
of one whole polypeptide chain.

4. The quaternary structure
Quaternary structure only exists, if there is more than one
polypeptide chain present in a complex protein. Then
quaternary structure describes the spatial organization of the
chains.

Enzyme
Enzyme is a biological catalyst is used to speed up the
rate of a reaction without being reacted.
Some enzymes have simple structure and the other most
complicated structure.
For the biological activity of enzymes require prosthetic
groups or so-called cofactors.
Cofactor is a nonprotein part of the enzyme.
Cofactors can be a simple metal ion,
Enzymes that have an organic molecule called
coenzyme cofactor.

Enzyme nomenclature
Enzymes are named according to the catalysis reaction, usually a
suffix to the name of the enzyme is-ase. It may be a common
name and refers to a class of enzymes that catalyse an common-
type reaction.
For example:
Polymerase: is an enzyme catalyzing the polymerization reaction.
Ascorbic acid oxidase: an enzyme that is mengkatalisi oxidation
of ascorbic acid.
Denaturation
Denaturation of a protein is
the loss of nature - the nature
of the protein structure by
disruption of hydrogen bonds.
Cause of denaturation:
The Changes of temperature
The Changes of pH
Protein analysis
1. Qualitative Analysis
Xantoprotein reaction
(tyrosine, phenylalalin,
tryptophan)
Hopkins-Cole reaction
(tryptophan)
Millon reaction
Nitroprusside reaction
(cysteine)
Sakaguchi reaction
(arginine)
2. Quantitatif Analysis
Kjeldahl method
Formol Titration method
Lowry method
Visible Spectometry
method (Biuret)
UV Spectometry method
(tyrosine, phenylalalin,
tryptophan)