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,
albumins)
Coordinated motion (actin and myosin).

Proteins
are the most
important buffers in
the body.

Mechanical support (collagen).

Immune protection (antibodies)
Generation and transmission of nerve impulses
- some amino acids act as neurotransmitters,
receptors for neurotransmitters, drugs, etc. are
protein in nature. (the acetylcholine receptor),
Control of growth and differentiation transcription factors
Hormones
growth factors ( insulin or thyroid stimulating
hormone)

Why?
(a)

Protein molecules
possess basic and
acidic groups which act
as H+ acceptors or
donors respectively if
H+ is added or removed.

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