Reviewer in Adv. Biology John Titus M.

Blancaver

Proteins

Proteins  Charged:
- They are composed of CHON oArginine (Arg)
- Help build and repair muscles oLysine (Lys)
- The monomers of protein are Amino oAspartic Acid (Asp)
Acids oGlutamic Acid ( Glu)
- Complete proteins contain adequate  Hydrophobic:
proportion of all 9 essential amino acids o Alanine (Ala)
necessary for the dietary needs of o Isoleucine (Ile)
humans and other animals. (Animal o Leucine (Leu)
proteins, Soya) o Phenylalanine (Phe)
o Valine (Val)
Amino acids o Proline (Pro)
- The monomers of proteins o Glycine (Gly)
- There are 20 in total, 9 of which are
• Essential amino acids - amino acids
essential amino acids
not produced by the body and are
• There 20 amino acids are:
taken from the food we eat
 Polar:
• The 9 essential amino acids are:
o Glutamine (Gln)
o Histidine
o Asparagine (Asn)
o Isoleucine
o Histidine (His)
o Leucine
o Serine (Ser)
o Lysine
o Threonine (Thr)
o Methionine
o Tyrosine (Tyr)
o Phenylalanine
o Csyteine (Cys)
o Threonine
o Methionine (Met)
o Tryptophan
o Trytophan (Trp)
o Valine

Functions of amino acids

1. Arginine – is converted into nitric oxide which helps blood vessels to relax and expand.
2. Lysine – concentrated in muscle tissue and helps in the absorption of calcium from the
intestinal tract, promotes bone growth.
3. Aspartic Acid – Major role in metabolism, plays a role in hormone production and for
normal nervous system function
4. Glutamic acid – important for protein synthesis
5. Glutamine – for biosynthesis of proteins
Reviewer in Adv. Biology John Titus M. Blancaver

6. Asparagine – involved in nerve and brain tissue function

7. Histidine – for growth and tissue repair
8. Serine - needed for fat metabolism, muscle growth
9. Threonine – for normal growth, maintain protein balance
10. Tyrosine – used in protein supplements to treat the inherited disease phenylketonuria
11. Cysteine - sulfur-containing, important structural and functional components of proteins
and enzymes
12. Methionine - prevent liver damage
13. Tryptophan - for normal growth of infants and nitrogen balance in adults
14. Alanine - involved in metabolism of tryptophan and pyridoxine
15. Isoleucine - increase endurance, repair muscle tissue
16. Leucine - for protein synthesis
17. Phenylalanine - makes the body healthy
18. Valine – for protein synthesis
19. Proline – plays important roles in protein synthesis and structure, metabolism, and
nutrition, as well as wound healing, antioxidative reactions, and immune responses.
20. Glycine - acts as neurotransmitter in central nervous system and it has many roles such
as antioxidant, anti-inflammatory, cryoprotective, and immunomodulatory in peripheral
and nervous tissues.
Notes:
1. Presentation didn’t include the functions of Proline and Glycine, so these are from the internet
2. Presentation says “trytophan” while other sources say “tryptophan”

Structure of proteins

Protein structure
- The basic functions of cells are entirely dependent upon the structure of their proteins
- The gene, or sequence of DNA, determines the unique sequence of amino acids in each
peptide chain.
- A change in nucleotide sequence of the gene's coding region may lead to a different amino
acid being added to the growing polypeptide chain, causing a change in protein
structure and therefore a change in function.
- An average protein has 300 amino acids
Reviewer in Adv. Biology John Titus M. Blancaver

(Tl;dr, The sequence of DNA changes the sequence of amino acids in a peptide chain, the
structure of proteins changes the functions of cells,)
1. Primary structure • is held together by peptide bonds
• refers to the linear sequence/chain of that are made during the process
amino acids in the polypeptide chain. of protein biosynthesis

2. Secondary structure
• Due to interactions (folding, coiling) of a polypeptide chain, proteins form a 3D shape
using weak hydrogen bonds.
• 2 types of secondary structures:

1. Alpha helix structure

– resembles a coiled spring and is
secured by hydrogen bonding
in the polypeptide chain.
– The length of the helix is
determined by certain amino
acids that will not participate in
these structures (ex. proline)

2. Beta Pleated sheet

– Appears to be folded or
pleated held together by
hydrogen bond between
polypeptide units that lie
adjacent to one another

(Note: Alpha Helix structure of protein is more stable than Beta pleated Sheet structure. It is
stabilized by the regular formation of hydrogen bonds.)

3. Tertiary structure
• The comprehensive 3D structure of a polypeptide chain of a protein
• Several types of bonds and forces hold a protein in its tertiary structure namely:
o Hydrophobic interactions o Hydrogen bond
Reviewer in Adv. Biology John Titus M. Blancaver

o Ionic bond o Van der Waals forces (distance-

o Disulfide bond (cysteine-cysteine) dependent)
• Secondary structures fold on themselves to form the tertiary structure of the protein
• Examples:

Chain B of Protein Kinase C MIL 1 Protein

4. Quaternary structure (take note of spelling)

• The association of multiple protein chains/subunits into a closely packed arrangement
• Some proteins are made up of several polypeptide subunits (like hemoglobin, it has 4
subunits, 2 alpha and 2 beta subunits)

Classification of Proteins

Classification based on:

1. Structure 2. Composition
a. Fibrous proteins a. Simple proteins
b. Globular proteins b. Conjugates proteins
c. Intermediate proteins
3. Functions
a. Catalytic e. Contractile
b. Storage f. Protective
c. Transport g. Toxins
d. Communication h. Structural

Classification based on structure

1. Fibrous protein
– Typically elongated and insoluble
– Involved in structure: tendons, ligaments, blood clots (Ex. Collagen in connective
tissues, keratin in hair, nails, feathers, and claws, fibrin in blood clots)
– Contractile proteins in movement: muscle, microtubules, cytoskeleton, mitotic
spindle, cilia, and flagella like actin and myosin

2. Globular protein
Reviewer in Adv. Biology John Titus M. Blancaver

– Are generally compact, soluble, and spherical in shape

– most proteins which move around (e.g. ovalbumin in egg, casein in milk)
– Proteins with binding sites: Enzymes, hemoglobin, immunoglobulins (Antibodies),
membrane receptor proteins

3. Intermediate Proteins
– Intermediate filaments (IFs), microfilaments (MFs), and microtubules (MTs) are the
key structural proteins that form the cytoskeleton.

Classification based on composition

Classification based on function

• CATALYTIC: enzymes (amylase, glucase, lipase, pepsin, trypsin, ATPase, sucrase, )
• STORAGE: ovalbumin (in eggs), casein (in milk), zein (in maize)
• TRANSPORT: hemoglobin, carrier proteins in cell membrane
• COMMUNICATION: hormones (e.g. insulin, glucagon, FSH, growth hormone,
neurotransmitters)
• CONTRACTILE: actin, myosin, dynein (in microtubules)
• PROTECTIVE: Immunoglobulin (antibodies), fibrinogen, fibrin (blood clotting factors)
• TOXINS: snake venom
• STRUCTURAL: cell membrane proteins, keratin (hair), collagen, fibroin in silk

Level of malnutrition

KWASHIORKOR - Also known as edematous malnutrition

- “The sickness the baby gets when the - Fluid retention (edema), enlarged liver
new baby comes”; also called “disease MARASMUS
of a deposed child” - worse condition than kwashiorkor
- due to inadequate protein intake
Reviewer in Adv. Biology John Titus M. Blancaver

- severe form of protein-energy - worst result of Anorexia nervosa (eating

malnutrition disorder)
- loss of body fat & muscle
Biuret test

What is the Biuret test?

- The Biuret test is performed on a sample to detect for the presence of protein, and the
peptide bonds in these proteins within said sample.
- A solution known as the Biuret solution/reagent is mixed with the analyte to determine
whether or not there are proteins as its constituents.
- A positive indication of this is a purple color change due to the binding of cupric ions from
the solution, with peptide bonds in the analyte.

Composition of the Biuret solution/reagent

a. Sodium hydroxide (NaOH)
– This acts as an alkaline base as to allow the chelation of proteins around a Copper (II)
ion.
b. Hydrated Copper (II) sulfate (CuSO4)
– This reacts with proteins to form a purple/lilac color.
c. Potassium Sodium tartrate (Rochelle salt, KNaC4H4O6·4H2O)
– This acts as the chelating agent for Copper (II) ions and stabilizes Copper (II) sulfate
(Formed from a weak acid and strong base, so it’s alkaline in nature)

Biuret reaction
There are 3 main components of the Biuret solution: Sodium hydroxide (NaOH), Hydrated
Copper (II) sulfate, and Rochelle salt. When the Biuret solution is mixed in a substance with
proteins as one of its constituents, Copper (II) ions form bonds with the nitrogen atoms present
in the protein’s peptide bonds to form a chelate complex. This chelate complex is able to reflect
a pale purple/lilac color, thus showing a positive indication. If the analyte has no proteins, no
color change takes place and the color remains the same, thus indicating a negative result.