PROTEIN

Anik Maunatin
• Protein adalah sumber asam-asam amino
yang mengandung unsur-unsur C, H, O, dan N
yang tidak dimiliki oleh lemak atau
karbohidrat.
• Sebagai zat pembangun, protein merupakan
bahan pembentuk jaringan-jaringan baru yang
selalu terjadi dalam tubuh dan
mempertahankan jaringan yang telah ada.
• Di dalam setiap sel yang hidup, protein
merupakan bagian yang sangat penting. Pada
sebagian besar jaringan tubuh, protein
merupakan komponen terbesar setelah air.
• Kekurangan protein dalam waktu lama dapat
mengganggu berbagai proses dalam tubuh
dan menurunkan daya tahan tubuh terhadap
penyakit.
• Protein dalam bahan makanan yang dikonsumsi
manusia akan diserap oleh usus dalam bentuk asam
amino
• Bila suatu protein dihidrolisis dengan asam, alkali,
atau enzim, akan dihasilkan campuran asam-asam
amino
• Sebuah asam amino terdiri dari gugus amino, sebuah
gugus hidroksil, sebuah atom hidrogen, dan gugus R
yang terikat pada sebuah atom C.
Protein adalah polimer
dari asam amino
 Amino Acids
• Arginine
• Histidine • Glycine
• Isoleucine • Proline
• Asparagine • Serine
•Tyrosine
• Aspartic Acid
• Tryptophan
• Cysteine • Valine
• Glutamic Acid • Methionine
• Alanine • Phenylalanine
• Leucine • Threonine
• Lysine • Glutamine

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 Essential Amino Acids
• Of the 20 amino acids that make up proteins
10 of them can be synthesized by the human
body. These amino acids are known as non-
Essential amino acids
• The other 10 amino acids must be acquired
from food sources. These amino acids are
known as essential amino acids

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 Essential Amino Acids

Essential amino acids Non-Essential amino acids

• Arginine • Alanine (from pyruvic acid)
• Histidine • Asparagine (from aspartic acid)
• Isoleucine • Aspartic Acid (from oxaloacetic acid)
• Leucine • Cysteine
• Lysine • Glutamic Acid (from oxoglutaric acid)
• Methionine
• Glutamine (from glutamic acid)
• Phenylalanine
• Glycine (from serine and threonine)
• Threonine
• Tryptophan • Proline (from glutamic acid)
• Valine • Serine (from glucose)
• Tyrosine (from phenylalanine)

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 Amino acid: Basic unit of protein

R
Different side chains,
- R, determin the
NH3 +
C COO properties of 20
Amino group Carboxylic
acid group amino acids.
H
An amino acid
 Amino Acids

Amino acids have both

• a carboxyl group
-COOH
• an amino group
-NH2
in the same molecule.. 

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 Classification of Amino Acids
• Classify by structure of R
– Nonpolar
– Polar
– Neutral
– Acidic
– Basic
 Amino Acids

Amino acids
forming proteins
may be
characterized as
Acidic, Basic, or
neutral
depending on the
character of the
side chain
attached.

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 Amino Acids are Amphoteric
• Amino acids are amphoteric. They are capable of behaving
as both an acid and a base, since they have both a proton
donor group and a proton acceptor group.

• In neutral aqueous solutions the proton typically migrates

from the carboxyl group to the amino group, leaving an ion
with both a (+) and a (-) charge.
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 Zwitter ion
• Acid-Base Properties of amino Acids
• Both the –NH2 and the –COOH groups in an amino acid
undergo ionization in water.
• At physiological pH (7.4), a zwitterion forms
– Both + and – charges
– Overall neutral
– Amphoteric
• Amino group is protonated
• Carboxyl group is deprotonated

• Isoelectric point (IEP) = is the pH at which the zwitter ion is

formed. Ex : IEP of alanine is 6
 The Zwitterion
This dipolar ion form is known as a Zwitterion.

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pH and ionization
 CH3 CH3
+
H3N–CH–COOH H2N–CH2–COO–
(1) (2)
The above structures :
(1) Alanine in acid.
(2) Alanine in base.

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 The Peptide Bond

- Each polypeptide chain starts on the left side by free amino group of the first amino acid enter
in chain formation . It is termed (N- terminus).
- Each polypeptide chain ends on the right side by free COOH group of the last amino acid and
termed (C-terminus).
 Peptides

• Amino acids linked by amide (peptide) bonds

Gly Lys Phe Arg Ser

H2N- -COOH
end Peptide bonds end

Glycyllysylphenylalanylarginylserine
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 Learning Check
Write the name of the following tetrapeptide using amino acid
names and three-letter abbreviations.
CH3
CH3 S
CH CH3 SH CH2
CH3 O CH O CH2 O CH2 O
-
H3N CH C N CH C N CH C N CH C O
H H H

Ala-Leu-Cys-Met
 Learning Check
• Draw the structural formula of each of the following peptides.
A. Methionylasparticacid
B. Alanyltryptophan
C. Methionylglutaminyllysine
D. Histidylglycylglutamylalanine
 Peptides
Dipeptide ( two amino acids joined by one peptide
bond): Example: Aspartame which acts as sweetening
agent being used in replacement of cane sugar. It is
composed of aspartic acid and phenyl alanine.
Tripeptides ( 3 amino acids linked by two peptide
bonds). Example: GSH which is formed from 3 amino
acids: glutamic acid, cysteine and glycine. It helps in
absorption of amino acids, protects against hemolysis
of RBC by breaking H2O2 which causes cell damage.

•
octapeptides: (8 amino acids)
Examples: Two hormones;
oxytocine and vasopressin (ADH).

polypeptides: 10- 50 amino acids: e.g. Insulin

hormone
 Protein size
• In general, proteins contain > 40 residues
– Minimum needed to fold into tertiary structure
• Usually 100-1000 residues
• Percent of each AA varies
• Proteins separated based on differences in size
and composition
• Proteins must be pure to analyze, determine
structure/function
Four Levels of Protein Structure
1. Primary Structure
2. Secondary Structure
3. Tertiary Structure
4. Quaternary Structure
 Primary Structure
• The unique sequence of amino acids.
• The sequence of amino acids are determined
by DNA.
Bentuk Primer
 Secondary Structure:
Common repeated coils and folds in the
polypeptide chains.
- Result from hydrogen bonds between the
amino and carboxyl groups of the a.a.
Two types:
- α helix (alpha): coiling
- β pleated sheet (beta): two or more regions
lying side by side
Bentuk sekunder
 Tertiary Structure
The overall shape resulting from interactions
between the sidechains (R groups)
Types of interactions:
• Hydrophobic (with surroundings)
• Hydrophilic (with surroundings)
• van der Waals
• Disulfide bridges
• Hydrogen Bonds
• Ionic bonds
Bentuk tersier
 Quaternary Structure
resulting from more than one polypeptide
interacting with each other.
Bentuk kuartener
 Protein berdasarkan komponen zat penyusunnya
(a). Protein sederhana.

1. Albumin: larut dalam air, contoh: putih telur, susu, (laktalbumin) dan sayuran.
2 Globulin: tidak larut dalam air, larut dalam pelarut garam netral encer, contoh: arachin dan
conarachin (kacang tanah), glicinin (kedele), laktoglobulin (susu), Inyosin dan actin (daging),
ovoglobulin (telur).
3. Glutelin: larut dalam pelarut alkali atau asam encer, tidak larut dalam garam netral atau
alkohol, contoh: glutenin (gandum). oryzenin (beras).
4. Prolamin: larut dalam alkohol, contoh: zein (jagung), gliadin (gandum).
5. Protamin: larut dalam air dan menggumpal karena panas, contoh: clupein (ikan kering).
skombrin (ikan mackerel).

(b). Protein majemuk (conyugated protein):Protein yang terikat oleh karbohidrat, lemak, asam
nukleat dll.

1. Fosfoprotein: Protein rnengandung gugus fosfat (susu dan kunig telur)

2. Lipoprotein: mengandung lemak dalam molekul protein (susu, telur dan darah)
3. Nukleoprotein: mengandung asam nukleat dalam protein (DNA, RNA, rRNA, inti sel)
4. Glikoprotein: mengandung karbohidrat dalam protein (ovolbumin pada telur)
5. Kromoprotein: mengandung pigmen dalam protein (myoglobin dalam daging).
6. Metaloprotein: protein yang membentuk komplek dengan metal: coalbumin (mengandung Co
dan Zn).
 Denaturation

Changing the confirmation of a protein/or the

ability for these interactions to occur can
make it non-functional.
Changes in pH, salt concentration, temperature
etc. can cause a protein to denature.
 DENATURING of PROTEINS
• Acid, alkaline, heat, alcohol, and agitation can
disrupt the chemical forces that stabilize
proteins and can cause them to lose their
shape (denature)
• Denaturing of proteins happens during food
preparation (cooking, whipping, adding acids)
or digestion (in the stomach with hydrochloric
acid)