Running head: TASK 3

Task 3: Protein Function

Name:
Institution:

Page 1 of 9

TASK 3

Part A
Model of hemoglobin showing how the molecule transports
oxygen

Figure 1
Hemoglobin
The protein inside red platelets:
(a) That conveys oxygen to cells and carbon dioxide to the lungs is hemoglobin
(b). Hemoglobin is comprised of four symmetrical subunits and four heme bunches. Iron
connected with the heme ties oxygen. It is the iron in hemoglobin that gives blood its red
shading.

Oxygenated versus deoxygenated hemoglobin states and their

differences
When hemoglobin is in an oxygenated (relaxed) state, it is referred to as oxyhemoglobin
(tense), while the deoxygenated state is called deoxygen-hemoglobin (CSUN, n.d.). The first
difference between the two forms is that the former is bound to oxygen, whereas deoxygenhemoglobin has a vacant oxygen binding site (CSUN, n.d.). Hemoglobin comprises of four
different polypeptide chains with iron being the oxygen binding site. In the relaxed state,
hemoglobin has a high affinity for oxygen, while the heterodimer interactions are weak. In

TASK 3

contrast, in the tense state, hemoglobin has a low affinity for oxygen and strong heterodimer
interactions.

Impact of pH on hemoglobins actions of binding and releasing

oxygen
pH is one of the factors that affect the way hemoglobin loads or unloads oxygen (ACC,
n.d). The higher the pH, the greater the affinity of hemoglobin for oxygen to keep it bound to the
former. Conversely, hemoglobin with a lower pH has a lower affinity to keep oxygen bound to
the hemoglobin and can, therefore, release more oxygen. As a result, hemoglobin delivers more
oxygen to body tissues at a lower pH (ACC, n.d.). The condition is known as the Bohr Effect.

Graph that illustrates the link between hemoglobins oxygen

binding and concentration at varying pH levels.

Fig 2
The red line demonstrates HEMOGLOBIN at the pH found in the lungs ... about pH 7.6.
The blue line demonstrates HEMOGLOBIN at the pH found in the fringe tissues ... about pH 7.2
The green line demonstrates MYOGLOBIN, which is found in muscle, clearly a fringe tissue.
High values for immersion imply that a high rate of the oxygen tying destinations in the
arrangement have oxygen bound to them. At the point when oxygen immersion values diminish,

TASK 3

this shows oxygen is being discharged from the coupling locales and turns out to be free,
disintegrated oxygen.

Diagrams that compare hemoglobins biochemical structure to

myoglobin

Figure 3
A. Hemoglobin arises as a tetrameric protein of which each subunit contains a globin near a
heme.
B. Myoglobin follows as a monomeric protein of which the globin nearby a heme.

TASK 3

Part B
Diagram illustrating the amino acid variations between normal
and sickle forms of hemoglobin

Figu
re 4

Diagram that shows the variations between sickle and healthy

red blood cells at the cellular level

TASK 3

Figure 5

3. How diseased and healthy red blood cells have varying

capacities for oxygen transportation
The shape of diseased cells is crescent moon-like due to the occurrence of protein
mutations. Healthy red blood cells possess a biconcave disk shape with a flat center. The disc
shape permits the cells to move more flexibly through blood vessels (whether large or small)
when delivering oxygen to all body tissues (NIH, 2015). The biconcave cells have an elastic
membrane as well as a high surface area to volume ratio that allows their flexible deformation.
As a result, the cells can go through tiny capillaries easily (Diez-Silva, Dao, Han et al., 2010, p.
382). However, unhealthy red blood cells can become stiff rods and take a crescent shape. They
ensue from slight or significant changes in the surface area that affect the deformability of the
cells (Diez-Silva et al., 2010, p. 382). The form of unhealthy cells is inflexible. As a result, it can
get attached to the walls of a blood vessel easily, resulting in a blockage (NIH, 2015). In effect,

TASK 3

this can either stop or slow down blood flow such that nearby tissues do not receive ample
oxygen (NIH, 2015).

Fig 6

4. a. Type of inheritance seen in sickle cell anemia

Children inherit sickle cell anemia through an autosomal recessive pattern, in which case,
a child receives genes from the ova (mother) and another corresponding set from the sperm
(father). A combination of these genes determines the childs traits. Sickle cell anemia is
determined by only a single gene pair passed down from each parent. Consequently, a child
inherits the condition when each parent transmits a mutated form of the gene. If the child
receives one defective copy as well as a good one, he or she becomes a carrier and rarely
experiences problems related to the mutated gene. Sickle cell genes control the production of
hemoglobin in the red blood cells. The primary task of hemoglobin is to carry oxygen to the
peripheral body tissues. If a child receives two sickle hemoglobin genes from each parent, the
outcome is the sickle cell disease. In most cases, children inherit the illness when both parents
carry the faulty hemoglobin gene or are sickle cell carriers. There is a one-in-four probability that
a child receives a pair of healthy genes. A similar possibility exists that a child will receive two

TASK 3

mutated genes. Finally, there is a one-in-two probability that a child will have the sickle trait by
receiving a healthy gene as well as a sickle one. The fact that there are existing sickle cell
children does not affect the chances of subsequent siblings as there is a one-in-four chance of the
sickle cell disease occurring for every conception.

Diagram demonstrating how sickle cell genes are transmitted

across generations

Figure 7

TASK 3

References
Austin Community College (ACC). (n.d.). The Bohr Effect. Retrieved from
www.austincc.edu/emeyerth/bohr.htm
California State University Northridge (CSUN). (n.d.). Hemoglobin. Retrieved from
www.csun.edu/~jm77307/Hemoglobin.pdf
Diez-Silva, M., Dao, M., Han, J., Lim, C. T., & Suresh, S. (2010). Shape and biomechanical
characteristics of human red blood cells in health and disease. MRS Bulletin, 35(05), 382388.
National Institute of Health (NIH). (2015). What is Sickle Cell Disease? Retrieved from
www.nhlbi.nih.gov/health/health-topics/topics/s