PROTEINS P2 REVIEWER -A mutation in gene can result in a change in the

primary acid sequence of a protein.

CELLULAR FUNCTION OF PROTEINS

Enzymes are biological catalyst –ex: Pepsin, Trypsin

Defense Proteins include antibodies (Immunoglobulins)
which are specific protein molecules produced by Secondary Structure of Proteins
specialized cells of the immune system in response to
foreign antigens.

-This level of structure describes the local folding

pattern of the polypeptide backbone and is stabilized
by hydrogen bonds between N-H and C=O groups. The
Transport Protein carry material from place to another most common are the orderly repeating forms known
in the body. Ex: transferrin, Hemoglobin and Myoglobin. as the a helix and the b sheet.
Regulatory Protein controls many aspects of cell -The secondary structure is the result of hydrogen
function, including metabolism and reproduction. Ex: bonding between the amide Hydrogen and carbonyl
Insulin and Glucagon oxygens of the peptide bonds.
Structural proteins provide mechanical support to large
animals and provide them with their outer coverings. Types of Secondary Structure
Ex: Keratin 1. α-Helix 2. β-Pleated Sheet
Movement Proteins are necessary for all forms of
movement. Ex. Actin and Myosin, Flagella of sperm cell. 1. α-Helix
Nutrient Protein serves as source of Amino acids for
embryos or infants. Ex: Albumin and Casein

PROTEIN STRUCTURE
Primary Structure of Proteins

The most common type of Secondary structure may it

be in coiled of helical conformation.
Special Feature:
-Every amide hydrogen and carbonyl oxygen associated
with the peptide backbone is involved in a hydrogen
bond when the chain coils into an α-Helix.
-It is the amino acid sequence of the protein chain. - Every carbonyl oxygen is hydrogen bonded to an
-This structure will determine its biological active form. amide hydrogen four amino acids away in the chain.
-It results from the covalent bonding between the Structural Property of a-helix
amino acids in the chain. - It has great mechanical strength and is applied very
-The amino acid sequence of a protein is encoded in efficiently in both the fibrous protein of skin and those
of muscle.
DNA. Proteins are synthesized by a series of steps called Proteins having an α-Helix structure
transcription (the use of a DNA strand to make a Fibrous Proteins – are structural proteins arranged
in fibers or sheets that have only one type of
complimentary messenger RNA strand - mRNA) and secondary structure.
translation (the mRNA sequence is used as a template α-Keratins – are fibrous proteins that form the
covering (hair, nails, and fur) of most land animals.
to guide the synthesis of the chain of amino acids
2. β-Pleated Sheet
which make up the protein).
The second common secondary structure in
-Genes can change by the process of mutation during
proteins resembles the pleated folds of drapery.
All the carbonyl oxygen and amide hydrogens in a
the course of evolution.
B-pleated sheet are involved in hydrogen bonds,
and the polypeptide chain is nearly completely sequences in a linear polypeptide together into a
extended. stable structure
The structure is maintained by the following
molecular interactions:
- Van der Waals Forces between the R groups of
non-polar amino acids that are hydrophobic.
- Hydrogen bonds between the polar R group of the
polar amino acids
- Ionic bonds (salt bridges) between the R groups of
Orientation of B-Pleated form oppositely charged amino acids
1. PARALLEL - Covalent bonds between the thiol-containing
-Beta sheets are parallel amino acids.
if the polypeptide strands run in the same
direction, N-terminus to C-terminus. The N- Globular proteins generally have a more compact
terminus of one beta strand will be opposite the N- and rounded shape and have functional roles (they
terminus of the other beta strand. do something)
-The parallel arrangement is less stable because the
geometry of the individual amino acid molecules Quaternary Structure
forces the hydrogen bonds to occur at an angle, • some proteins are made up of multiple
making them longer and thus weaker. polypeptide chains, also known as subunits. When
2. ANTI-PARALLEL these subunits come together, they give the
-Beta sheets are anti-parallel protein its quaternary structure.
if the polypeptide strands run in opposite • The forces that hold the quaternary structure of a
directions. The N- terminus of one beta strand will protein are the same as those that hold the tertiary
be opposite the C-terminus of the other beta structure.
strand. • Prosthetic group – when a non-protein group is
-In the anti-parallel arrangement, the hydrogen added to the functional protein. Ex: Glycoprotein
bonds are aligned directly opposite each other,
making for stronger and more stable bonds.
-An anti-parallel beta-pleated sheet forms when a
polypeptide chain sharply reverses direction. This
can occur in the presence of two consecutive
proline residues, which create an angled kink in the
polypeptide chain and bend it back upon itself.

Silk Fibroin
- A protein whose structure is an antiparallel B-
pleated sheet.
- The polypeptide chains of a B-pleated sheet are PROTEIN DIGESTION
almost completely extended, and silk does not • Is the degradation of protein by cellular enzymes
stretch easily. in a process called hydrolysis.
- Glycine accounts for nearly half of the amino acids • The macromolecules are the proteins or
of silk fibroin. Alanine and serine account for most polypeptides themselves, and the subunits are the
of the others, amino acids.
• It takes place in two different phases: - In the
Tertiary Structure of Proteins stomach
- In the small intestine.
Both of these phases of digestion are based on
several types of enzymes that are called
Proteinases and Proteases.
• Proteases –endo & exo peptidases:
- Enzymes that degrade proteins by hydrolysis of
peptide bonds
Tertiary structure is the complete three- • Proteinases- endo peptidases; proteases that
dimensional (3-D) structure of a polypeptide. It is show specificity for intact proteins
formed spontaneously and stabilized both by side
chain interactions and, in extracellular proteins, by
disulfide bonds. This folding brings distant
 Coagulation- occur as the protein molecules unfold
and become entangled. At this point, they are no
longer in solution; they have aggregated to become
a solid.

Protein Digestion in Mouth & Salivary Glands • pH

-Chewing and crushing rich foods and mix them A high concentration of hydrogen ions (low pH) will
with saliva to be swallowed. result in more groups being protonated. Carboxyl
groups (aspartic acid, glutamic acid, the carboxy
Protein Digestion in Stomach terminus) and phenolic groups are uncharged when
- It is the start of protein digestion. protonated. The nitrogen groups (amines on lysine,
• Gastrin – Stimulates Parietal cells to secrete HCl; guanidino of arginine, and imidazole in histidine,
Chief cells of the gastric glands to secrete etc.) are charged when protonated
pepsinogen • Organic Solvents
• HCl / Hydrochloric Acid – Denatures protein -Polar organic solvents, such as rubbing alcohol (2-
structure. Activates pepsinogen (Zymogen) to propanol), denatured proteins by disrupting
pepsin. hydrogen bonds within the protein, in addition to
• Pepsin- Hydrolyzes proteins to smaller forming hydrogen bonds with the solvent, water
polypeptides and some free amino acids. Nonpolar regions of these solvents interfere with
hydrophobic interactions in the interior of the
Protein Digestion in Intestine protein molecules, thereby disrupting the
• The remainder of protein digestion occur in the conformation.
small intestine as the result of the action of • Heavy metals
enzymes such as trypsin (secreted by the pancreas) - Mercury (Hg2+) or Lead (Pb2+) may form
and peptidases (located in the cells that line the negatively charged side chain groups.
small intestine). - Heavy metals may also bind to sulfhydryl groups
• Secretin – Stimulates the pancreas to secrete of a protein that can accompanied by loss of
bicarbonate into the small intestine to neutralize function.
the gastric HCl • Detergents
• Cholecystokinin- Stimulates secretion of several Detergent have hydrophobic region and
pancreatic enzyme with activity optima pH 7 to 8. hydrophilic. When detergents interact with
• Trypsin proteins, they disrupt hydrophobic interactions,
- Activates Chymotrpsinogen →chymotrypsin causing the protein chain to unfold.
- Further hydrolyze the peptides that were • Mechanical Stress
produced by pepsin in the stomach specifically the - Stirring, whipping, or shaking can disrupt the
peptide bonds next to Lys and Arg. weak interactions that maintain protein
• Chymotrypsin - Cleaves peptide bonds next to conformation. This is the reason that whipping egg
Phe, Tyr, Trp, Met, Asp and His whites produces a stiff meringue.

Denaturation of Protein
• Occur when the organized structures of a
globular protein, the a-helix, the B-pleated sheet
and tertiary folds become completely disorganized.
However, it does not alter the primary structure.
Factors that cause Denaturation
• Temperature
As the temperature increase, molecular movement
also increase and the bonds within the cells vibrate
more violently which results to disruption of
protein structure.