PINES CITY COLLEGES

COLLEGE OF MEDICAL LABORATORY SCIENCE

1st SEMESTER A.Y. 2023-2024

BIOCHEMISTRY 201

Lesson Number 3:
PROTEINS
Learning Objectives:
At the end of the lesson, you should be able to:
1. enumerate the general characteristics of proteins.
2. diagram the general structure of amino acids.
3. Describe the physical properties of amino acids.
4. Identify and characterize the different classification of amino acids.

GENERAL CHARACTERISTICS OF PROTEINS ➢ Colorless crystalline substance soluble in

➢ Carbon, hydrogen, oxygen, and water.
nitrogen CHON ➢ Insoluble in organic solvents with a high
➢ The most abundant macromolecule in melting point.
Ig or
immunoglobulin-
made up of
the body. ➢ Essential amino acids:
proteins is ➢ Mostly synthesized by the liver o Isoleucine
- I leucine so

synthesise in
plasma cells henylalanine ↑

➢ Water soluble Can be dissolve in water o Phenylalanine

~
Leucine
➢ Amphoteric Can be positively and negatively charge o Leucine
- ↳yeine
➢ Amino acids as the building blocks. o Threonine Tryptophan
Threonine
~
o Lysine Methionine
AMINO ACIDS: THE BUILDING BLOCKS o Tryptophan Valine

➢ Organic compound Any compounds that contain carbon o Methionine

➢ Contains amino group (-NH2) and o Valine
Carboxylic acid group (-COOH)
➢ General structure ➢ PHYSICAL PROPERTIES OF AMINO ACIDS
1. Solubility
Peptide bonds- links the bond of
proteins. o Longer aliphatic side chains
Aminoglycosides- -Y (leucine & valine): less soluble
destroys the Glycosidic bond if carbohydrates
peptide bonds o Shorter chains (glycine &
GA
alanine): increased solubility

➢ Held by peptide bonds/amide linkages.

2. Melting point
More than
o >200°C
3. Taste GAYS
o Sweet: glycine, alanine, valine,
serine
o Tasteless: leucine

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 o Bitter: isoleucine
4. Appearance
o White crystalline

C. Essential and non-essential

5. UV absorption spectrum of aromatic D. Basic
amino acids 1. Lysine LAH

o Tryptophan, tyrosine & 2. Arginine

phenylalanine absorbs UV light. 3. Histidine
6. Optical properties E. Acidic
o Alpha carbon atoms of all the 1. Aspartic acid AG
amino acids except glycine are 2. Glutamic acid
asymmetric, so they show optical F. Imino: contains both imine and carboxyl
activity functional groups.
o Vary according to the pH of the 1. Proline Plt

solution. 2. Hydroxyproline
7. Acid-base properties
o In aqueous solution, they
become ionized that can act as
acid or base.
All enzymes in the body
is made up of proteins
➢ CLASSIFICATION OF AMINO ACIDS
A. Neutral: monoamine-monocarboxylic BIOLOGICAL FUNCTION OF PROTEINS
1. Straight chain: glycine, alanine, 1. Enzymatic catalysis – all known enzymes are
serine, threonine GAST proteins Transport oxygen
2. Branched chain: valine, leucine, 2. Transport proteins – hemoglobin in RBC Common in
isoleucine VIL milk
3. Nutrient proteins – albumin & casein
Egg white
4. Storage proteins – ferritin
5. Contractile proteins – actin and myosin Found in blood.
6. Structural proteins Found in muscles Stores iron

a. Collagen – tendons and cartilage , Gives strength

b. Elastin – ligaments Gives elasticity
c. Keratin – hair & fingernails
B. Aromatic: with phenyl hydroxyphenyl or
d. Fibrin – silk fibers and spider webs
indole rings substituted on alanine
7. Defense proteins
1. Phenylalanine: contains the phenyl
a. Immunoglobulins or antibodies IF
ring
b. Prothrombin and fibrinogen Serves as clotting protein
2. Tyrosine: contains the hydroxyphenyl
8. Regulatory proteins – polypeptides or
ring
peptide hormones
3. Tryptophan: contains the indole ring

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 CLASSIFICATION OF PROTEINS o Examples: histones of
I. SIMPLE PROTEINS nucleoproteins, globin of
➢ Proteins that upon hydrolysis yield only hemoglobin
amino acids or their derivatives 7. Protamines
1. Albumin o Simplest of the proteins
o Soluble in water, coagulated by o Regarded as large polypeptides.
heat. o Strongly basic and yield chiefly
o Example: Lactalbumin from milk, basic amino acids upon
ovalbumin from egg white hydrolysis, particularly arginine.
2. Globulin o Major nuclear sperm proteins.
o Insoluble in water, coagulated by o Originally isolated from the sperm
Multiple myeloma or heat. of salmon fish.
bone marrow cancer o Example: ovoglobulin of egg o Example: protamine medication
yolk, serum globulin Neutralises heparin to
prevent bleeding
3. Glutelins II. CONJUGATED PROTEINS
o soluble in dilute acids and alkali, ➢ Composed of simple proteins combined
insoluble in neutral solvents, with some non-protein substances
coagulated by heat. called as prosthetic group.
o Example: Glutamine of wheat, 1. Nucleoprotein
oryzenin of rice o Prosthetic group: nucleic acid
4. Prolamines of gliadins o Found in cell nuclei
o soluble, plant proteins (seeds) o Chief constituent of chromatin
o Example: Zein of corn, gliadin of 2. Glycoprotein and mucoproteins
wheat o Prosthetic group: carbohydrates
5. Scleroproteins of albuminoids (mucopolysaccharides)
o the least soluble of the proteins o Glycoproteins contain <4% CH2O
o insoluble in water, salt solutions, o Mucoproteins contains >4% CH2O
dilute acids and alkali, and 3. Phosphoproteins
alcohols. o Prosthetic group: Phosphoric acid
o Entirely animal protein o Casein in milk
o Chief constituents of exoskeletal 4. Chromoproteins
structures such as hair, horn, o Prosthetic group: pigment
hoofs, and nails and of the o Heme of hemoglobin
organic materials of the 5. Lipoproteins
cartilage and bones. o Simple conjugated lipids such as
o Found in supportive tissues. phospholipids and cholesterol
o Principal class: collagen and 6. Metalloproteins
keratins. o Prosthetic group: metals (Fe, Cu,
6. Histones Mn)
Thalassemia- genetic
o High in basic amino acids o Copper of ceruloplasmin
disorder. Can not make o Occur in combination with the
hemoglobin
nucleic acids in the nuclei of the
somatic cells of many
organisms.

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COMPILED AND PREPARED BY:
Luiza D. Botengan, RMT

REFERENCES:
Bishop, M. L., Fody, E.P., Schoeff, L.E. (2018).
Clinical Chemistry: Principles, Techniques
and Correlations. (8th ed.) Philadelphia:
Lippincott Williams & Wilkins, Baltimore,
Maryland. H. Stephen Stoker (2017).
Biochemistry, 3rd edition. C&E, Publishing,
Inc.: South Triangle, Quezon City

Maricris Realubin – Ubalde (2019). Biochemistry

for Allied Health Sciences. Edric Publishing
House: Sta. Cruz, Manila

Todd A. Swanson et al. (2010). Biochemistry,

Molecular Biology, and Genetics.
Lippincott Williams & Wilkins: Philadelphia,
PA 19106

Google Images

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