Chapter 1

Protein
 Contents

 1. Chemical components
 2. Molecular structures
 3. Structure-function relationship
 4. Physical and chemical properties
 5. Metabolism proteins
What are proteins?

Proteins are macromolecules

composed of amino acids linked
together through peptide bonds.
 Element components of
proteins
 major elements
C, H, O, N, S.
 trace elements
P, Fe, Cu, Zn, I, …
 The average nitrogen content in
proteins is about 16%.

The protein quantity can be estimated.

protein in 100g sample = N per gram x 6.25 x 100

The basic building blocks of proteins

Amino Acids
only 20 types of amino acids
are used for protein synthesis
in biological systems.

L-α-Amino acid
L-α-Amino acid
Classification of amino acid
A Classification of
Amino Acids
 Amino acids are grouped as
(1) non-polar, hydrophobic;
(2) polar, neutral;
(3) acidic;
(4) basic.
 Peptide

A peptide is a compound of
amino acids linked together
by peptide bonds.
 peptide bond
A peptide bond is a covalent bond formed
between the carboxyl group of one AA and the
amino group of its next AA with the elimination
of one H2O molecule.
Biologically active peptides
Glutathione (GSH)
As a reductant to protect nucleic
acids and proteins
Peptide hormones
Neuropeptides responsible for signal
transduction
From primary to quaternary structure
 Protein classification
 Constituents
simple protein
conjugated protein = protein +
prosthetic groups

Overall shape
Globular protein
Fibrous protein
Fibrous VS Globular
 Protein darah :
albumin : menjaga tekanan osmosis
protrombin dan fibrinogen : proses pembekuan darah
gamma- globulin : kekebalan
 Protein struktur :
Kuku, tanduk, rambut, otot, bagian non mineral gigi dan
tulang

Sebagai enzim : katalisator

Pengaturan proses-proses : hormon
Section 4 Physical and Chemical
Properties of Proteins
1. Amphoter
 isoelectric point (IEP)
 The pH at which the protein has
zero net-charge is referred to as
isoelectric point (IEP)
 3 Protein denaturation
renaturation, precipitation
DENATURASI PROTEIN
and coagulation
 Molekul protein dapat pula mengendap peristiwa
koagulasi

 Faktor-faktor penyebab denaturasi protein :

- perubahan pH : penggumpalan kasein
- Panas : merusak ikatan hidrogen dan jembatan garam
- Radiasi : sinar X dan U.V
- Pelarut organik : aseton, alkohol.
- Garam-garam dari logam berat : Ag2+, Hg2+, Pb2+
- Pereaksi-pereaksi alkaloid : asam tannat, asam pikrat
- Salting Out : NaCl, Asam sulfosalisilat, Na2SO4, NH4(SO4),
Fenol
 4 UV absorption

 Trp, Tyr, and Phe have aromatic

groups of resonance double bonds.
 Proteins have a strong absorption
at 280nm
 5 Coloring reactions

 Biuret reaction
 Ninhydrin reaction
 Xantoprotein reaction
Section 5 Exploration of
Protein
 Isolation and purification
• Centrifugation
• Dialysis
• Precipitation
• Chromatography
• Electrophoresis
Electrophoresis:
separation of polar compounds based on their
mobility through a solid support. The separation is
based on charge (pI) or molecular mass.

+ _

+ _
_ _ _ _ + + + +
26
Metabolisme
Transaminasi

GOT
Transaminasi

GPT
Metabolisme
 Oksidasi Asam Amino

 Pada umumnya, degradasi asam amino dimulai dengan

pelepasan gugus amino menghasilkan kerangka C
diubah mjd senyawa antara metabolisme utama tubuh
 Metabolisme asam amino pada umumnya terjadi di hati
 Kelebihan di luar liver dibawa ke hati diekskresikan
 Ammonia
 Digunakan kembali utk proses biosintesis

 Diekskresi scr langsung atau diubah terlebih dahulu mjd

asam urat / urea

Function: detoxification of ammonia
(prevents hyperammonemia)
 TERIMAKASIH
 Lipid
(Triasilgiserol)
Senyawa-
senyawa steroid
a b

h
Asam lemak
Kolesterol

c d
g

Asetil Ko A Badan Keton

f
e
ATP CO2 + H2O
 b