1. Alemar Allecer BSMT-2A
Assignment: Hemoglobin
Title: Sickle Cell Anemia Brochure/ Web Page
Goals: To have students relate protein structure with protein function or
malfunction
Objectives:
At the end of the lesson, students will be able to:
1. Explain the structure of Hb
2. Explain the role of Hb in oxygen transport
3. Explain the role of Hb in sickle cell anemia
Purpose: Hemoglobin is the main oxygen transport molecule in
mammals, including humans. The structure of the molecule is quite
important; a small mutation can result in non-functional Hb molecules,
or those that work in an abnormal fashion, as is the case with sickle cell
anemia. Students need to constantly identify the relationship of structure
to function, and can do so using this important molecule.
Materials/ Resources:
Web links:
• http://www.nlm.nih.gov/medlineplus/ency/article/000527.htm
• http://sickle.bwh.harvard.edu/hemoglobin.html
• http://web.indstate.edu/thcme/mwking/hemoglobin-
myoglobin.html
• http://www.cties.niu.edu/Practice%20Problems/Protein
%20structure/hemoglobin.htm
• http://tutor.lscf.ucsb.edu/instdev/sears/biochemistry/tw-
hbn/hemoglobin-properties.htm
• http://www.people.virginia.edu/~rjh9u/oxytrans.html

2. 1.WHAT IS SICKLE CELL ANEMIA? WHAT ARE THE
SYMPTOMS, AND THE PROBLEMS THAT PRESENT IN
CASES OF SCA?
Sickle cell anemia Sickle cell anemia is a disease passed down through families
in which red blood cells form an abnormal sickle or crescent shape. Red blood
cells carry oxygen to the body and are normally shaped like a disc.
Symptoms/ problems Related to Sickle Cell Anemia?
The most common symptom of anemia is fatigue (feeling tired or weak). Other
signs and symptoms of anemia include:
Shortness of breath
Dizziness
Headaches
Coldness in the hands and feet
Paler than normal skin or mucous membranes (the tissue that lines your nose,
mouth, and other organs and body cavities)
Jaundice (a yellowish color of the skin or whites of the eyes)
2.WHAT CAUSES SCA? CAN ANYONE GET IT, OR ARE YOU BORN
WITH IT? (BE SPECIFIC- YOU WANT TO TELL EXACTLY WHAT IS
MUTATED!)

3. Sickle cell anemia is an inherited disease. People who have the disease inherit two
genes for sickle hemoglobin—one from each parent.
Symptoms usually do not occur until after age 4 months.
Almost all patients with sickle
cell anemia have painful The following symptoms may
episodes (called crises), which occur because small blood
can last from hours to days. vessels may become blocked
These crises can cause pain in by the abnormal cells:
the bones of the back, the long Painful and prolonged erection
bones, and the chest. (priapism)
Poor eyesight or blindness
Some patients have one Problems thinking or confusion
episode every few years. caused by small storkes
Others have many episodes per Ulcers on the lower legs (in
year. The crises can be severe adolescents and adults)
enough to require a hospital
stay. Over time, the spleen no longer
works. As a result, people with
When the anemia becomes sickle cell anemia may have
more severe, symptoms may symptoms of infections such
include: as:
Fatigue Bone infection (osteomyelitis)
Paleness Gallbladder infection
Rapid heart rate (cholecystitis)
Shortness of breath Lung infection (pneumonia)
Yellowing of the eyes and skin Urinary tract infection
(jaundice)
Other symptoms include:
Younger children with sickle Delayed growth and puberty
cell anemia have attacks of Painful joints caused by
abdominal pain. arthritis

4. 3.WHAT IS BLOOD? (THE TYPES OF CELLS PRESENT AND THEIR
FUNCTIONS, IN BRIEF)
Blood is a combination of plasma (watery liquid) and cells that float in
it. It is a specialized bodily fluid that supplies essentials substances and
nutrients, such as sugar, oxygen, and hormones to our cells, and carries
waste away from those cells, this waste is eventually flushed out of the
body in urine, feces, sweat, and lungs (carbon dioxide). Blood also
contains clotting agents.
Plasma is a mixture of water, sugar, fat, protein, and
potassium and calcium salts. It also contains many
chemicals that help form blood the clots necessary to
stop bleeding. More than 92% of plasma is water.
TYPES OF BLOOD CELLS: (FUNCTION )
Red blood cells also known as RBCs or erythrocytes.
They are shaped like slightly indented, flattened disks.
These are the most abundant cells, and contain
hemoglobin (Hb or Hgb).
.
White blood cells (leukocytes) - these are the cells of
our immune system; they defend the body against
infections and foreign materials. Lymphocytes and
ganulocytes (types of white blood cells) can move in and
out of the bloodstream to reach affected areas of tissue..
Platelets (thrombocytes) - are involved in the clotting
(coagulation) of blood. When we bleed the platelets clump
together to help form a clot.

5. 4.WHAT DOES HB LOOK LIKE?(WHAT IS IT MADE FROM – TELL
ABOUT IT’S STRUCTURE)
Hemoglobin is a protein that is carried by red c.lls. It picks up oxygen in the
lungs and delivers it to the peripheral tissues to maintain the viability of cells.
Hemoglobin is made from two similar proteins that "stick together". Both
proteins must be present for the hemoglobin to pick up and release oxygen
normally. One of the component proteins is called alpha, the other is beta.
Before birth, the beta protein is not expressed. A hemoglobin protein found
only during fetal development, called gamma, substitutes up until birth.
Protein Structure
Primary Structure: The unique sequence of amino acids
that makes up a protein or polypeptide chain.
Secondary Structure : The way in which the primary
structure of a polypeptide chain folds.
Tertiary Structure: The final 3D structure of a protein,
entailing the shaping of a secondary structure.
Quaternary Structure: The structure formed when two
or more polypeptide chains join together, sometimes with an inorganic
component, to form a protein.

6. 5.WHAT ROLE DOES HB PLAY IN OXYGEN TRANSPORT? (BE SPECIFIC-
TELL HOW MANY OXYGEN ARE HELD, AND WHAT HOLDS THEM)
is the iron-containing oxygen- Hemoglobin has an oxygen
transport metalloprotein in the binding capacity of 1.34 mL O2
red blood cells of all per gram of hemoglobin,[4] which
vertebrates[1] (with the increases the total blood oxygen
exception of the fish family capacity seventy-fold compared
Channichthyidae[2]) as well as the to dissolved oxygen in blood.
tissues of some invertebrates.
The mammalian hemoglobin
Hemoglobin in the blood carries
molecule can bind (carry) up to
oxygen from the respiratory
four oxygen
organs (lungs or gills) to the rest
molecules.Hemoglobin is involved
of the body (i.e. the tissues)
in the transport of other gases: it
where it releases the oxygen to
carries some of the body's
burn nutrients to provide energy
respiratory carbon dioxide (about
to power the functions of the
10% of the total) as
organism, and collects the
carbaminohemoglobin, in which
resultant carbon dioxide to bring
CO2 is bound to the globin
it back to the respiratory organs
protein. The molecule also carries
to be dispensed from the
the important regulatory
organism.In mammals, the
molecule nitric oxide bound to a
protein makes up about 97% of
globin protein thiol group,
the red blood cells' dry content,
releasing it at the same time as
and around 35% of the total
oxygen.Hemoglobin is also found
content (including water).[3]

7. outside red blood cells and their
progenitor lines. Other cells that
QUIZ.
contain hemoglobin include the
A9 dopaminergic neurons in the 0. Which a.a can react with itself
substantia nigra, macrophages, to form a dimmer by formation of
disulfide bond? Cysteine
alveolar cells, and mesangial cells
in the kidney. In these tissues,
hemoglobin has a non-oxygen-
1. Cysteine is one of the 2 sulfur-
carrying function as an containing amino acids. What is
antioxidant and a regulator of the other one? Methionine
iron metabolism.
Hemoglobin and hemoglobin-like
2. What is the 1 letter code for
molecules are also found in many
phenylalanine? F
invertebrates, fungi, and plants.
In these organisms, hemoglobins
may carry oxygen, or they may act 3. Which amino acid differs from
to transport and regulate other Ala in that one of the methylene H
things such as carbon dioxide, is replaced by a hydroxyl group?
nitric oxide, hydrogen sulfide and Serine
sulfide. A variant of the molecule,
called leghemoglobin, is used to
scavenge oxygen away from 4. Serine are one of the 2 non-
anaerobic systems, such as the aromatic hydroxyl a.a.. What is
the other one?
nitrogen-fixing nodules of
Threonine
leguminous plants, before the
oxygen can poison the system.
5. Threonine is one of 2 aliphatic
hydroxyl amino acids. What is the
other one? Serine
6. Threonine differs from serine
by having a methyl subsituent in
place of one of the hydrogens on
which carbon? 3 carbon

8. 7. Serine and Threonine are the 12. Is leucine considered an
two hydroxyl amino acids. They internal or external aminoi acid?
are commonly considered Internal
hydrophilic or hydrophobic? Is
hydrophilic due to the
hydrogen bonding capacity of 13. Isoleucine is one of two amino
the hydroxyl group acids that have two chiral centers.
What is the other one? Threonine
8. Which of the following amino
acids is referred to as branched 14. Leucine and valine are two of
chain amino acid? Arg, Leu, Tyr? the three amino acids having
Leucine : Arginine is a basic branched hydrocarbon side
amino acid and it is not
chains. What is the third one?
branched): (Tyrosine is an Isoleucine
aromatic amino acid)
15. Methionine is one of two
9. Valine is usually found in the sulfur-containing a.a.. What is the
interior or exterior of proteins? other one? Cysteine
Internal. Hydrophobic amino
acids tend to bury themselves
inside protein molecules.
16. Is the methionine considered
an internal or external amino
acid? Internal. Hydrophobic
10. Valine is usually found in the amino acids tend to bury
interior or exterior of proteins? themselves inside protein
Interior. Hydrophobic amino molecules.
acids prefer to bury themselves
inside protein molecules.
17. Which amino acid is alanine
with one of the beta-hydrogens
11. 2 amino acids have one replaced by a carboxylic group?
additional methylene group in aspartic acid
their side chain compared with
valine. Can you name one of
them? either Leucine or
Isoleucine 18. Glutamic acid is one of the
two acidic amino acids. What is
the other one? aspartic acid

9. 19. Glutamic acid is one of the 27. ..is a derivative of alanine with
two acidic amino acids. What is a phenyl substituent on the beta-
the other one? aspartic acid carbon. Phenylalanine
20. Which amino acid has one 28. There are 3 aromatic amino
additional methylene group in its acids. Phenylalanine, tryptophan
side chain than does aspartic and? Tyrosine
acid? glutamic acid
29. Which amino acid is derived
21. ..is the amide of aspartic acid. from phenylalanine by
Asparagines hydroxylation in the para position?
Tyrosine
22…is the amide of glutamic acid.
Glutamine 30. Which is the largest of the
amino acids? Tryptophan
23. ..is a commonly site for
attachment of carbohydrates in a 31. The basic a.a Lys, Arg, His
glycoproteins. Asparagine are normally found in the interior
or exterior part of proteins?
external.
24. .. has an additional single
methylene group in the side chian
relative to asparagine. Glutamine
25. Which amino acid has one
methylene group LESS than
glutamine in its side chain?
asparagine
26. Which amino acid has a
secondary amino group rather
than a primary alpha-amino
group? Praline

10. 19. Glutamic acid is one of the 27. ..is a derivative of alanine with
two acidic amino acids. What is a phenyl substituent on the beta-
the other one? aspartic acid carbon. Phenylalanine
20. Which amino acid has one 28. There are 3 aromatic amino
additional methylene group in its acids. Phenylalanine, tryptophan
side chain than does aspartic and? Tyrosine
acid? glutamic acid
29. Which amino acid is derived
21. ..is the amide of aspartic acid. from phenylalanine by
Asparagines hydroxylation in the para position?
Tyrosine
22…is the amide of glutamic acid.
Glutamine 30. Which is the largest of the
amino acids? Tryptophan
23. ..is a commonly site for
attachment of carbohydrates in a 31. The basic a.a Lys, Arg, His
glycoproteins. Asparagine are normally found in the interior
or exterior part of proteins?
external.
24. .. has an additional single
methylene group in the side chian
relative to asparagine. Glutamine
25. Which amino acid has one
methylene group LESS than
glutamine in its side chain?
asparagine
26. Which amino acid has a
secondary amino group rather
than a primary alpha-amino
group? Praline