rantai dari
molekul glukosa dan gula lainnya
yang berulang
Lemak (Lipid) :
Memiliki
struktur yang terbentuk dari satu
molekul gliserol dan tiga molekul
asam lemak
Protein :
Protein
Terdapat
Amino Acids - 1
Amino Acids - 2
ION ZWITTER
2.
pH TINGGI :
GUGUS KARBOKSIL TERDISOSIASI
3.
pH RENDAH :
GUGUS AMINO TERDISOSIASI
4.
pH ISOLEKTRIK Protein
STRUKTUR PROTEIN
1. STRUKTUR PRIMER
struktur linear yang tersusun dari ikatan
polipeptida
2. STRUKTUR SEKUNDER
Pelipatan struktur primer dari suatu polipeptida
3. STRUKTUR TERSIER
Pelipatan dari struktur-struktur sekunder
membentuk suatu bentuk yang khas
4. STRUKTUR KUARTENER
Struktur kompleks gabungan dari beberapa
struktur tersier suatu polipeptida
Primary
Assembly
Secondary
Folding
Tertiary
Packing
Quaternary
Interaction
PROCESS
STRUCTURE
Biology/Chemistry of Protein
Structure
Struktur primer
Struktur sekund
(alpha helix)
Klasifikasi Protein
1. BERDASARKAN SUSUNAN
MOLEKUL
Endapan
Hitam
PEMURNIAN PROTEIN :
1. BERDASARKAN UKURAN MOLEKUL
Menggunakan Membran
SEMIPERMIABLE atau KROMATOGRAFI
KOLOM
2. BERDASARKAN MUATAN PROTEIN
Menggunakan KROMATOGRAFI
PENUKAR ION (ION EXCHANGE
Chromatography)
Ammonium Sulfate
Precipitation
Very high ionic
strength Proteins
precipitate Salting Out
Modest
Purification but
Also Useful to
Concentrate
the Sample
Column Chromatography
Flow-through
Eluate
Ion-Exchange Chromatography
Positively
CH2-COO
+
charged (basic)
If these groups are basic in nature, they interact with
negatively
charged
molecules and are called anion
+
protein
or enzyme
exchangers.
CH2-COO
+
CM cellulose
cation exchanger
-
Negatively
charged (acidic)
protein or enzyme
CH2-COO-
+
+
CH2-COO- +
CM cellulose
cation exchanger
Negatively
charged proteins
pass through the
column
CH2-COO +
+ Increasing
[NaCl] of the
elution buffer
CM cellulose
cation exchanger
CH2-COO
CM cellulose
cation exchanger
+
- Na Na+2
- Na+
CH2-COO
Na+2
ClCl- +
+
Cl
+
- +
Cl
Affinity Chromatography
Characteristic
Procedure
Solubility:
1.
2.
Salting in
Salting out
Ionic charge:
1.
2.
3.
Polarity:
1.
2.
Adsorption chromatography
Paper chromatography
Reverse-phase chromatography
Hydrophobic interaction
chromatography
Molecular size:
1.
2.
Dialysis
Gel electrophoresis
Gel filtration chromatography
Ultracentrifugation
Binding specificity:
1.
Affinity chromatography