STRUKTUR & FUNGSI

PROTEIN

Evi Umayah Ulfa

PROTEIN
 Asal kata “PROTEIOS” = UTAMA
 Makromolekul yang tersusun atas Asam Amino yang
disatukan oleh ikatan peptida
 Monomer : Asam-Amino 20 macam

Human Insulin
Berat Molekul

Dalton:
Unit masa yang nilainya sebanding
dengan atom hidrogen

Gly C2NO2H5 75
Ala C3NO2H7 89
Val C5NO2H11 117
Leu C6NO2H13 131
Ile C6NO2H13 131
 Peranan Protein
Motion
(myosin, actin)

Defense
Material
transport (Hb) (antibodies,
toxins)

PROTEIN

Replication
and repairing
Mechanical of genetic
(Collagen) information
(DNA and RNA
polymerases)

Metabolism
(enzymes)
Klasifikasi Protein

1.
KOMPOSISINYA

2. 3.
BENTUKNYA FUNGSI
BIOLOGIS
 1. Komposisinya
 Protein sederhana (simple) : bila
hihidrolisis hanya menghasilkan asam
amino

 Protein konjugat (cojugated) : bila

dihidrolisis tidak hanya menghasilkan asam
amino saja, tetapi juga komponen organik
atau anorganik lainnya (gugus prostetik)
Macam-macam protein konjugat

Macam protein Gugus prostetik

1. Nukleo protein (ribosom, Tobacco RNA
mosaic virus)
2. Lipoprotein (plasma 1-lipoprotein) Phospholipid, kolesterol, lipid netral
3. Glikoprotein
#  Globulin Heksosamin, galaktosa, manosa
# Plasma orosomucoid Galaktosa, manosa, N-asetil-
galaktosamin,
4. Phosphoprotein (Kasein) Phosphate
5. Hemo protein (Hemoglobin, Fe-protoporphyrin
sitokrom C dan Katalase )
6. Flavoprotein (suksinat dehidro Flavin adenin dinukleotida (FAD)
genase, D-amino acid oxidase)
7. Metalloprotein
# Ferritin Fe(OH)2
# Sitokrom oksidase Fe dan Cu
# Alkohol dehidrogenase Zn
# Xanthine oxidase Mo dan Fe
2. Bentuknya
 Fiber (Fibrous)
Rantai poli-peptida yg disusun secara paralel.
Secara fisik protein ini kuat, tidak larut dalam
air, larut dalam larutan garam.
 Globular
Rantai polipeptidanya dilipat-lipat dgn kuat
sehingga berbentuk seperti bulat bundar.
 Fibrous proteins have a structural role
Collagen fibers are a major portion of
tendons, bone and skin. Alpha helices of
collagen make up a triple helix structure
giving it tough and flexible properties.

•Fibroin fibers make the silk spun by

spiders and silk worms stronger weight
for weight than steel! The soft and
flexible properties come from the beta
structure.

•Keratin is a tough insoluble protein that

makes up the quills of echidna, your hair
and nails and the rattle of a rattle snake.
The structure comes from alpha helices
that are cross-linked by disulfide bonds.

Source:http://www.prideofindia.net/images/nails.jpg 9
http://opbs.okstate.edu/~petracek/2002%20protein%20structure%20function/CH06/Fig%2006-12.GIF
http://my.webmd.com/hw/health_guide_atoz/zm2662.asp?printing=true
The globular proteins
Cell motility
Myosin (red) and actin filaments (green) in
coordinated muscle contraction

Organic catalysts in biochemical reactions

– enzymes

2 2 +

Regulatory proteins – hormones,

transcription factors
Insulin binds to cell membranes and this
triggers the cells to absorb glucose for use
or for storage as glycogen in the liver.
The globular proteins
Cell motility – proteins link together to form
filaments which make movement possible.

Organic catalysts in biochemical reactions –

enzymes

Regulatory proteins – hormones, transcription

factors

Membrane proteins – MHC markers, protein

channels, gap junctions

Defense against pathogens – poisons/toxins,

antibodies, complement

Transport and storage – hemoglobin and myosin

3. Fungsi Biologis

1 Enzim Alcohol dehydrogenase, lipase, DNA Pol

2 Protein simpan - Ovalbumin (protein putih telur)

(storage) - Casein (protein susu)
- Zein (protein biji jagung)

3 Protein transport - Hemoglobin (transport O2 dlm darah)

- Myoglobin (transport O2 dlm otot)
- Serum albumin (transport AL dalam arah)

4 Protein gerak Myosin dan actin( prot gerak pada otot)

(kontraktil)
3. Fungsi Biologis

5 Protein - Antibodi
perlindungan - fibrinogen
(protective) - thrombin
6 Hormon - insulin
- hormon tumbuh
- represor

7 Protein Struktural -coat protein virus

-Keratin
-Collagen
- Elastin
Anatomy of an amino acid
 The R groups, also called side chains,
make each AA unique and distinctive.
 R groups are different in their size, charge,
hydrogen bonding capability and chemical
reactivity.
 Aas are grouped as (1) non-polar,
hydrophobic; (2) polar, neutral; (3) basic;
and (4) acidic.
 Non-polar and hydrophobic AAs

R groups are
non-polar,
hydrophobi
c aliphatic
or aromatic
groups.

R groups are
uncharged.

AAs are
insoluble in
H2O.
Polar and uncharged AAs

R groups are polar:

-OH, -SH, and -NH2. R groups are highly
reactive.

R AAs are soluble in H2O, that

is, hydrophilic.
 Basic Aas/ Positively Charged AAs

 R groups have one -

NH2.
 R groups are
positively charged at
neutral pH (=7.0).
 AAs are highly
hydrophilic.
Acidic AAs

 R groups have –
COOH.
 R groups are
negatively charged
at physiological pH
(=7.4).
 AAs are soluble in
H2O.
Polypeptide
Backbone
Levels of Protein Structure
Primary structure

Two peptides of 21 and 30 AAs

Two inter-chain -S-S- bonds
One intra-chain -S-S- bond
Secondary Structure

 The secondary structure of a

protein results from hydrogen
bonds at regular intervals
along the polypeptide
backbone.
 Alpha helix
 beta pleated sheets

 Beta turn

 Random coil
Hydrogen Bonds in Proteins

 H-bonds form between 1) atoms involved in the peptide

bond; 2) peptide bond atoms and R groups; 3) R
groups
 Helix
 Formed by a H-bond
between every 4th peptide
bond – C=O to N-H
 Usually in proteins that span
a membrane
 The  helix can either coil to
the right or the left
 Can also coil around each
other – coiled-coil shape – a
framework for structural
proteins such as nails and
skin
 Sheets

 Core of many proteins is

the  sheet
 Form rigid structures with
the H-bond
 Can be of 2 types
 Anti-parallel – run in an
opposite direction of its
neighbor (A)
 Parallel – run in the same
direction with longer looping
sections between them (B)
  turns

• -turns allow the protein backbone to make abrupt turns.

• Again, the propensity of a peptide for forming -turns depends on its sequence.
 The structural properties of silk are due to beta
pleated sheets.
 The presence of so many hydrogen bonds makes each silk
fiber stronger than steel.
Tertiary Structure

 Tertiary structure is determined by a variety of

interactions among R groups and between R groups
and the polypeptide backbone.
 These interactions
include hydrogen
bonds among polar
and/or charged
areas, ionic bonds
between charged
R groups, and
hydrophobic
interactions and
van der Waals
interactions among
hydrophobic R
groups.
 While these three
interactions are relatively
weak, disulfide bridges,
strong covalent bonds that
form between the
sulfhydryl groups (SH) of
cysteine monomers,
stabilize the structure.
 Quaternary Structure

 Quarternary structure results

from the aggregation of two
or more polypeptide subunits.
 Collagen is a fibrous protein of
three polypeptides that are
supercoiled like a rope.
 This provides the structural strength
for their role in connective tissue.
 Hemoglobin is a
globular protein
with two copies
of two kinds
of polypeptides.
 Examples of other quaternary
structures
Tetramer Hexamer Filament

SSB DNA helicase Recombinase

Allows coordinated Allows coordinated DNA binding Allows complete
DNA binding and ATP hydrolysis coverage of an
extended molecule
 Example of quaternary structure -
Sir1/Orc1 heterodimer

Example is Sir1/Orc1 complex solved at UW: Hou, Bernstein, Fox, and Keck
(2005) Proc. Natl. Acad. Sci. 102, 8489-94.
 A protein’s conformation can change in response to the
physical and chemical conditions.
 Changes in pH, salt concentration, temperature, or
other factors can unravel or denature a protein.
 These forces disrupt the hydrogen bonds, ionic bonds, and
disulfide bridges that maintain the protein’s shape.
 Some proteins can return to their functional shape
after denaturation, but others cannot, especially in the
crowded environment of the cell.
 Usually denaturation is permanent
 SINTESIS PROTEIN

DNA
Transkripsi
Eukariotik
Prosesing mRNA mRNA
• Capping ‘5 Translasi
• Tailing ‘3
• Splicing Polipeptida/
Pre protein
Post Translasi
Protein