Protein

Harliansyah, Ph.D
Bagian Biokimia FK Univ YARSI
2014
Naming of Peptides
• For naming peptides, the AA suffixes – ine
(glycine), - an (tryptophan) ate (glutamate) are
changed to –yl with the exception of C –
terminal AA.

 A tripeptide composed of an N – terminal

glutamate, a cysteine and a C – terminal
glycine is called:
glutamyl – cysteinyl - glycine
 Function of proteins
• Enzymatic catalysis
• Transport and storage (the protein hemoglobin,
Proteins
albumins)
• Coordinated motion (actin and myosin). are the most
important buffers in
• Mechanical support (collagen). the body.

• Immune protection (antibodies)

• Generation and transmission of nerve impulses

- some amino acids act as neurotransmitters,
Why?
receptors for neurotransmitters, drugs, etc. are
protein in nature. (the acetylcholine receptor), (a) Protein molecules
possess basic and
• Control of growth and differentiation - acidic groups which act
as H+ acceptors or
transcription factors donors respectively if
Hormones H+ is added or removed.
growth factors ( insulin or thyroid stimulating
hormone)
Peptides of Physiologic Importance
1. Glutamine (Glutathione)
- a tripeptide composed
of 3 AA
- gamma – glutamyl –
cysteinyl glycine
- wildly distributed in
nature
- exists in reduced or
oxidized states
Functions:
a) As a coenzyme for certain enzymes as
prostaglandin PGE2 synthase
glycoxylase
b) Prevents the oxidation of sulfhydryl groups of several proteins
to disulfide groups
c) In association with glutathione reductase participates in the
formation of correct disulfide bonds in several protiens
d) In erythrocytes
- maintains RBC membrane structure and
integrity
- protects hemoglobin from getting oxidized by agents
such as H2O2
e) Involved in the transport of AA in the
intestine and kidney tubules via delta –
glutamyl cycle or Meister cycle

f) Involved in the detoxification process

g) Toxic amounts of peroxidases and free

radicals produced in the cells are
scavanged by glutathione peroxidase ( a
selenium containing enzyme).
2. Thyrotropin Releasing Hormone (TRH)
- a tripeptide secreted by hypothalamus
Function:
Stimulate pituitary gland to release thyrotropic hormone

3. Oxytocin
- contains 9 AA (nonapeptide)
- hormone secreted by posterior
pituitary gland
Function:
Stimulate contraction of the uterus muscle during
delivery

Stimulate contraction of muscle in breasts for milk

ejection
 - they differ in their
physicochemical properties
which ultimately determine
the characteristics of proteins
 Hemoglobin – Structure
• Heme – Center is Iron (4 per molecule
• Iron binds to the oxygen – 1 per Iron
• 250 million Hb per cell
 Hemoglobin Properties
• At the tertiary level, the surface residues of the a and b
subunits form complementary sites that promote tetramer
formation (a2b2), the normal physiological form of
hemoglobin.
• Contains 4 heme groups, so up to 4 O2 can be bound
• Its physiological role is as a carrier/transporter of oxygen from
the lungs to the rest of the body, therefore its oxygen binding
affinity is much lower than that of myoglobin.
• If the Fe2+ becomes oxidized to Fe3+ by chemicals or
oxidants, oxygen can no longer bind, called Methemoglobin