BIOKIMIA I

Dr. rer.nat. Lalu Rudyat Telly Savalas

Maulida Septiyana M.Si
 Rule of This Class
 Biokimia I, 3 SKS ( 2 Pertemuan di Kelas, 1 Praktikum)
 Total Pertemuan : 14 + 2 (6 pertemuan sebelum UTS + 1 )
 Ujian Final : 2 kali (UTS dan UAS)
 Tugas Besar : 1 Kali
 Kuis : Beberapa kali
 Minimum Absensi 75%
 BIOKIMIA
• Biokimia adalah ilmu yang mempelajari struktur, organisasi,
dan fungsi materi hidup pada tingkat molekul.
• Biokimiawan mempertanyakan:
– Bagaimana struktur kimia dari materi hidup?
– Bagaimana interaksi dari materi hidup sehingga dapat membentuk
supramolekul, sel, jaringan multisel dan organisma?
– Bagaimana materi hidup dapat mengambil energi dari lingkungan?
– Bagaimana organisma dapat menyimpan dan meneruskan informasi
yang diperlukan untuk pertumbuhan dan reproduksi?
– Perubahan kimia apa yang menyertai reproduksi, penuaan, kematian
sel atau organisma?
– Bagaimana reaksi kimia dikendalikan di dalam sel?
Pembagian kajian biokimia

Struktur &
Fungsi Biomolekul

Informasi
Metabolisme
Genetika
Biokimia sebagai interdisiplin ilmu

Kedokteran
Nutrisi
Kimia organik

Genetik Biokimia Mikrobiologi

Biofisik Fisiologi
Biologi sel
 Biokimia sebagai ilmu kimia
Untuk memahami peran biokimia pada biologi,
maka diperlukan pemahaman mengenai:
• Unsur-unsur kimia penyusun biomolekul,
• Struktur dan fungsi dari ratusan senyawa
biomolekul,
• Peran biomolekul dalam reaksi metabolisme
termasuk stoikiometri dan mekanisme
reaksinya.
 CONTENTS:
• Asam amino
• Peptida dan Protein
• DNA, RNA, dan Biosintesis Protein
• Enzim, Kinetika Michelish-Manten, Inhibisi
Enzim
• Isolasi, Pemurnian, dan Karakterisasi Enzim
• Hormon, Virus Regulasi Enzim, dan Integrasi
Topik Biokimia
 Amino Acid???

Protein DNA

Macromolecules Carbohydrate

Lipid
Protein as Macromolecules

Amino Acid
 Amino Acid
Carboxyl

a
Amino
 Common Features of Amino Acids
 There are 20 "standard" amino acids that are specified by
the genetic code and polymerized into proteins by
ribosomal translation.
 All amino acids contain an a carbon to which typically 4
different substituent groups are attached
 These groups are the a-amino group, the a-carboxyl group,
hydrogen, and the variable R group (side-chain). (Note that
in glycine, the R group consists of another hydrogen atom.
In the other 19 amino acids the a carbon is a chiral center.)
 The a-amino and a-carboxyl groups are charged at neutral
pH.
 There are two possible configurations for these four
substituents--the "D" and "L" stereoisomers, which are
mirror images of each other (enantiomers)
 The standard amino acids have the L-configuration. Amino
acids are classified based on the characteristics of their R
groups.
Non polar
Aromatic Polar uncharged
 Polar positive Polar negative

b
g

d
e
 Numbering of Carbons in Amino Acids
The conventions for labeling the carbon atoms in amino acids is
illustrated using lysine in the figure. The a carbon is always carbon-2 of
the amino acid. The a-carboxyl group is always carbon-1
 Zwitterions
A zwitterion
• has an equal number of —NH3+ and COO– groups
• forms when the H from —COOH in an amino acid transfers to the
—NH2
 Isoelectric Point (pI)
The isoelectric points (pI)
• are the pH at which zwitterions have an overall zero charge
• of nonpolar and polar (neutral) amino acids exist at pH values
from 5.1 to 6.3

At this point, the net charge is zero. The AA is least soluble in water and the AA does not
migrate in electric field (important in electrophoretic separation of peptides)
18
 Zwitterions in Acidic Solutions
In solutions that are more acidic than the pI,
• the COO– in the zwitterion accepts a proton
• the amino acid has a positive charge
Glycine, with a pI of 6.0, has a 1+ charge in solutions that have a
pH below pH 6.0.

19
 Zwitterions in Basic Solutions
In solutions that are more basic than the pI,
• the NH3+ in the zwitterion loses a proton
• the amino acid has a negative charge
Glycine, with a pI of 6.0, has a 1– charge in solutions
that have a pH above pH 6.0.

20
Uncommon amino acids
 pI

Each amino acid has a characteristic isoelectric point which is the pH at

which the positive equals the negative charge. This varies based on the side
chain.
For amino acid without ionizable side chains (non-polar), the Isoelectric Point
(equivalence point, pI) is pI= pK1+pK2/2

At this point, the net charge is zero. The AA is least soluble in water and
the AA does not migrate in electric field (important in electrophoretic
separation of peptides)