Republic of the Philippines

Pamantasan ng Cabuyao
(University of Cabuyao)
College of Health and Allied Sciences
Katapatan Mutual Homes, Brgy. Banay-banay, City of Cabuyao, Laguna 4025

BIOCHEMISTRY
CHMN104A

(MIDTERM PERIOD)

MIDTERM RESEARCH
THE MONOMERS

Members: ALONZO, TRISTAN RAINE

ARANDA, SHERLYN

CAPONES, ANGELICA

LEYVA, RANCI ANNE

PARALA, MERRY CHRIST

PEÑANO, MARY KRISTINE AMBER

PROFESSOR: JERRY B. SANGUILLOSA

APRIL 16, 2023

 Please answer every question as concisely as possible. Indicate your references.

1. Complete the table by giving 3 medicinally important proteins with their molecular weight,
functions or roles, and the clinical condition when the protein is absent or at an abnormal level.
Please briefly describe the clinical condition.

Protein Molecular Number of Chemical Location in Roles/Functions Clinical Condition

Weight polypeptide Formula the Body
chain

Insulin ~5.8 kDa 2 C254H377N Produced by Regulates glucose Diabetes mellitus,

65O75S6 beta cells in homeostasis by a metabolic
the pancreas promoting glucose disorder
uptake by cells, characterized by
inhibiting high blood glucose
gluconeogenesis, levels due to
and promoting insufficient insulin
glycogen synthesis. production or
resistance to its
effects.

Hemoglobin ~64 kDa 4 C2952H4664 Found in red Binds to oxygen in Anemia, a

N812O832S8 blood cells the lungs and condition
Fe4 transports it to the characterized by
body's tissues, low levels of
while also aiding hemoglobin in the
in the removal of blood, resulting in
carbon dioxide. reduced
oxygen-carrying
capacity and
symptoms such as
fatigue, weakness,
and shortness of
breath.

Fibrinogen ~340 kDa 3 C4892H7712 Produced by Essential for blood Bleeding

N1312O1460 the liver and clotting, as it is disorders, such as
S42 found in blood converted into hemophilia or von
plasma fibrin during the Willebrand
coagulation disease, which are
process, which characterized by
forms a mesh-like abnormal bleeding
network that due to a deficiency
stabilizes the clot. in fibrinogen or
other clotting
factors.

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2. What is currently the largest known protein? Give its molecular weight, location in the body,
function/role, and chemical formula.

Name of the largest known protein: Titin (contraction for Titan protein) (also known as connectin) is a
protein that is encoded by the TTN gene in humans.

Molecular weight: Titin is the largest known protein; its human variant consists of 34,350 amino acids,
with the molecular weight of the mature "canonical" isoform of the protein being approximately
3,816,030.05 Da.

Location in the body: Titin is primarily found in the muscles of many animals, including humans.
Specifically, it is located in the sarcomeres of muscle cells, which are the basic units of muscle
contraction. The human titin gene is situated on the long arm of chromosome 2 and comprises 363 exons
that code for 38,138 amino acid residues (4200 kDa)

Function/role: Titin's key duties are to stabilize the thick filament, center it between the thin filaments,
prevent sarcomere overstretching, and recoil the sarcomere once it has been stretched like a spring.

Chemical Formula: The protein's empirical chemical formula is C169,719H270,466N45,688O52,238S911.

3. a. What is the smallest protein in the human body?

Tripeptide glutathione, also known as gamma-glutamyl-cysteinyl-glycine, is the smallest protein in the

human body and contains only three amino acids. One of the most crucial molecules in our bodies,
proteins have a variety of roles in cellular structure, function, and communication. From tiny peptides
with only a few amino acids to huge protein complexes with hundreds of subunits, proteins may range
widely in size and complexity. Glutathione, a tripeptide with only three amino acids, is one of the tiniest
proteins in the human body.

b. Where is it located?

Almost every cell in the human body has glutathione, both in the cytoplasm and the nucleus. While
being very little, glutathione is extremely important for keeping our cells healthy and functioning. Its
main job is to act as an antioxidant and detoxifying agent, shielding cells from dangerous pollutants and
oxidative stress.

c. What is its role/function?

Its main role is as an antioxidant and detoxifying agent, protecting cells from oxidative stress and
harmful toxins.

d. Provide the full amino acid sequence in three-letter abbreviation.

The full amino acid sequence of glutathione is: gamma-glutamyl-cysteinyl-glycine or γ-Glu-Cys-Gly

(in three-letter abbreviation). Glutathione functions by disarming dangerous chemicals like reactive
oxygen species (ROS) and free radicals that may destroy cells and cause a variety of illnesses, including
cancer, Alzheimer's, and heart disease. Moreover, glutathione controls how cells grow and divide and
helps to control how the immune system reacts.

e. Provide the full amino acid sequence in one-letter abbreviation.

2
 The full amino acid sequence of glutathione is gamma-glutamyl-cysteinyl-glycine, or γ-Glu-Cys-Gly
in three-letter abbreviation. The amino acids are represented by the one-letter acronym G-Glu-Cys-Gly.
With its sulfur-containing cysteine residue, glutathione has a special structure that enables it to establish
powerful connections with heavy metals and other toxins, aiding in their elimination from the body.

4. What protein name is derived from Pikachu? Who discovered it? Where it can be found? What
is its role or function?

Protein name derived from Pikachu: The protein name derived from Pikachu is called Pikachurin. It is
an extracellular matrix-like retinal protein and named after Pikachu, a species of the Pokémon franchise.
The name of this protein was inspired by pikachu’s “lightning-fast moves” , because they observed that
the protein had a "flashing" effect on the electrical signals in the retina, and also because it "hangs"
between the photoreceptor cells and the bipolar cells in the retina, connecting them together.

Location: Pikachurin is a protein found in the retina of the eye and is involved in the transmission of
visual information from the photoreceptor cells to the bipolar cells.

Who discovered it: It was discovered by a team of researchers led by Dr. Takahisa Furukawa at Osaka
University in Japan in 2008. The discovery was published in the scientific journal Nature, in a paper titled
"Pikachurin, a dystroglycan ligand, is essential for photoreceptor ribbon synapse formation".

Function: Pikachurin facilitates the transfer of vision signals from photoreceptor cells to bipolar cells in
the retina, which is its duty or function.

A protein called plikachurin binds to the protein dystroglycan, which is present on the surface of the
photoreceptor cells in the retina. The creation of specialized structures known as ribbon synapses, which
enable the effective transmission of visual information from photoreceptor cells to bipolar cells, depends
on this interaction.

Pikachurin aids in the organization of calcium channels in the ribbon synapses and controls the flow of
calcium ions, both of which are essential for the release of neurotransmitters that alert the brain to the
presence of visual inputs. Without Pikachurin, the ribbon synapses do not develop properly, which
disrupts the transfer of visual information and causes significant vision impairment.

Pikachurin's overall purpose is to support the transfer of visual impulses from the retina to the brain,
hence ensuring the proper operation of the visual system.

5. Show the relationship among carbohydrates, obesity, and diabetes.

Obesity, diabetes, and carbohydrates are all closely related to one another.

A crucial macronutrient that gives the body energy is carbohydrates. Bread, rice, pasta, fruits,
vegetables, and sweets are just a few of the many foods that contain them. When ingested, carbohydrates
are converted to glucose, which the body uses as its main energy source.

Obesity is a condition when a person has too much body fat, which can cause health issues. Fat is
produced when a person consumes more calories than they expend via everyday exercise and normal life.
If the energy from the carbohydrates is not used up, eating an excessive amount of them might result in
weight gain and obesity.

3
Diabetes is a long-term illness in which the body struggles to efficiently control blood sugar levels. Type
1 and type 2 diabetes are the two primary subtypes. When the body does not create enough insulin, a
hormone that controls blood sugar levels, type 1 diabetes develops. When the body develops an insulin
resistance or is unable to produce enough insulin to control blood sugar levels, type 2 diabetes results.

Particularly in those with diabetes, carbohydrates can significantly affect blood sugar levels. For those
with diabetes, a surge in blood sugar levels brought on by an excessive intake of carbohydrates can be
harmful. Consistently high blood sugar levels can eventually result in concerns like nerve, kidney, and
eyesight issues.

In summary, excessive consumption of carbohydrates can contribute to weight gain and obesity, which
can increase the risk of developing type 2 diabetes. Additionally, carbohydrates can have a significant
impact on blood sugar levels, which can be particularly problematic for individuals with diabetes.
Therefore, it is important to consume carbohydrates in moderation and maintain a healthy diet to prevent
obesity and manage diabetes effectively.

6. What is the glycemic index? Provide its importance.

The glycemic index (GI) measures how rapidly a food containing carbohydrates raises blood sugar
levels in the body. Higher scores indicate a faster and greater increase in blood sugar levels. It grades
foods on a scale of 0 to 100 depending on their impact on blood sugar levels.

The value of the glycemic index rests in its capacity to assist consumers in making educated decisions
about the foods they consume and how those choices will affect their blood sugar levels. Foods with a
high glycemic index (high GI) cause blood sugar levels to rise quickly, which may boost insulin
production. This might result in hunger pangs and desires for more high GI foods. In addition to
increasing the risk of insulin resistance, weight gain, and other health issues, this rollercoaster effect on
blood sugar levels can be dangerous for those who already have diabetes or are at risk of getting it.

People can assist control their blood sugar levels by consuming foods that have a lower GI, which can
have a variety of positive health effects, such as greater insulin sensitivity, a decreased risk of type 2
diabetes, and better weight management. However, it is important to remember that the glycemic index
should only be one aspect to take into account when choosing a diet. Other aspects, such as the total
amount of nutrients in a dish, serving sizes, and cooking techniques, should also be considered.

7. Differentiate between the lock-and-key model and the induced-fit model of enzymes.

The lock-and-key model and the induced-fit model are two different theories used to explain how
enzymes interact with their substrates.

In contrast to the lock and key model, which assumes that the enzyme's active site is the complement of
the substrate and thus precisely fits to the substrate, the induced fit model assumes that the enzyme's
active site does not completely fit to the substrate. Additionally, the lock and key model describes the
selectivity of the enzyme's active site to a particular substrate, whereas the induced fit model assumes that
the enzyme's active site must undergo a conformational shift to increase binding.

8. Explain the factors that affect the rate of enzymatic reactions.

4
 Enzymatic reactions are chemical reactions that are catalyzed by enzymes, which are proteins that
increase the rate of the reaction. The rate of an enzymatic reaction can be affected by several factors,
including:

● Temperature: Enzymes work optimally at a specific temperature range. If the temperature is too
low, the reaction rate will be slow. If the temperature is too high, the enzyme may denature and
lose its function.
● pH: Enzymes also work optimally at a specific pH range. A change in pH can alter the shape of
the enzyme and affect its ability to catalyze the reaction.
● Substrate concentration: The rate of an enzymatic reaction increases as the concentration of
substrate increases until a saturation point is reached. At this point, the reaction rate remains
constant even if more substrate is added.
● Enzyme concentration: Increasing the concentration of enzyme can increase the rate of the
reaction, as long as there is sufficient substrate.
● Inhibitors: Inhibitors can decrease the rate of an enzymatic reaction by binding to the enzyme
and preventing it from catalyzing the reaction.
● Activators: Activators can increase the rate of an enzymatic reaction by binding to the enzyme
and increasing its catalytic activity.
● Presence of cofactors or coenzymes: Some enzymes require cofactors or coenzymes to function.
The absence or deficiency of these factors can decrease the rate of the reaction.

Understanding the factors that affect the rate of enzymatic reactions is important in optimizing the
conditions for enzymatic reactions, as well as in developing drugs that target specific enzymes.

REFERENCES:

Alberts, B., Johnson, A., Lewis, J., Raff, M., Roberts, K., & Walter, P. (2014). Molecular biology of the
cell. Garland Science.

American Diabetes Association. Diabetes Basics: https://www.diabetes.org/diabetes

American Diabetes Association. (2021). Glycemic index and diabetes. Retrieved from
https://www.diabetes.org/nutrition/healthy-food-choices-made-easy/glycemic-index-and-diabetes

Berg, J. M., Tymoczko, J. L., & Stryer, L. (2002). Biochemistry. WH Freeman.

Brand-Miller, J., & Buyken, A. E. (2012). The glycemic index issue. Current Opinion in Lipidology,
23(1), 62-67. doi: 10.1097/MOL.0b013e32834dccc6

Centers for Disease Control and Prevention. Obesity: https://www.cdc.gov/obesity/index.html

Fersht, A. (1999). Structure and mechanism in protein science: a guide to enzyme catalysis and protein
folding. WH Freeman.

Foster-Powell, K., Holt, S. H., & Brand-Miller, J. C. (2002). International table of glycemic index and
glycemic load values: 2002. The American Journal of Clinical Nutrition, 76(1), 5-56. doi:
10.1093/ajcn/76.1.5

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Harvard T.H. Chan School of Public Health. Carbohydrates:
https://www.hsph.harvard.edu/nutritionsource/carbohydrates/

Jenkins, D. J., Kendall, C. W., Augustin, L. S., Mitchell, S., Sahye-Pudaruth, S., Blanco Mejia, S., ... &
Josse, R. G. (2017). Glycemic index: Overview of implications in health and disease. The American
Journal of Clinical Nutrition, 105(3), 757-777. doi: 10.3945/ajcn.116.145153

Jencks, W. P. (1987). Catalysis in chemistry and enzymology. Dover Publications.

Koshland Jr, D. E. (1958). Application of a theory of enzyme specificity to protein synthesis. Proceedings
of the National Academy of Sciences, 44(2), 98-104.

Mayo Clinic. Diabetes:

https://www.mayoclinic.org/diseases-conditions/diabetes/symptoms-causes/syc-20371444

Nelson, D. L., & Cox, M. M. (2008). Lehninger principles of biochemistry. Macmillan.

"Pikachurin, a dystroglycan ligand, is essential for photoreceptor ribbon synapse formation" - Omori,
Yoshihiro et al. Nature. 2008 May 22; 453(7194): 645-649. DOI: 10.1038/nature06879.

"Pikachurin regulates synaptic transmission by regulating the transport of vesicle-associated proteins" -

Ueno, Shuichi et al. Journal of Neuroscience. 2018 Apr 11; 38(15): 3753-3769. DOI:
10.1523/JNEUROSCI.2935-17.2018.

"Pikachurin, a dystroglycan ligand, is essential for photoreceptor ribbon synapse formation in the retina" -
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Voet, D., Voet, J. G., & Pratt, C. W. (2016). Fundamentals of biochemistry: life at the molecular level.
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https://www.sciencedirect.com/topics/agricultural-and-biological-sciences/tripeptide

https://www.sciencedirect.com/topics/chemistry/glutathione

http://www.eurekaselect.com/169663/article

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