Proteins, Amino Acids, and

Enzymes
 Protein Structures
1. Primary Structure
The sequence of amino acids present in a protein's peptide chain or chains.

2. Secondary Structure
The regularly repeating ordered spatial arrangements of amino acids near
each other in the protein chain.

a. Alpha helix
Hydrogen bonds between fourth amino acid
b. Beta pleated sheet
Hydrogen bonds between two side-by-side chains, or single chain that is folded back itself.
3. Tertiary Structure
The overall three-dimensional shape that result from attractive
forces between amino acid chains
4. Quaternary Structure
The three-dimensional shape of a protein consisting of two or
more independent peptide chains, which results from non-covalent
interactions between R groups.
COMPARISON OF FIBROUS AND GLOBULAR
PROTEINS

Fibrous Globular

Shape Long and narrow Round/spherical

Purpose Structural Functional

Solubility Insoluble in water Soluble in water

Collagen, myosin, fibrin, Enzymes, haemoglobin,

Examples
actin, keratin, elastin insulin, immunoglobulin
 Enzymes
• Enzymes are globular proteins that serve as catalysts of biochemical
reactions.
• The reactant or substrate binds to the hydrophobic cleft within the
enzyme called the active site which serves as its catalytic site. This
process results to the formation of an enzyme-substrate complex
(ES) that eventually dissociates to form the product and recover the
enzyme after the reaction.
 Enzymatic Action
1. The enzyme and the substrate are in the same area.
Some situations have more than one substrate molecule that the
enzyme will change.

2. The enzyme grabs on to the substrate at a special area called the

active site.
The combination is called the enzyme/substrate complex. Enzymes
are very, very specific and don't just grab on to any molecule.
3. A process called catalysis happens.
Catalysis is when the substrate is charged. It could be broken
down or combined with another molecule to make something new. It
will break or build chemical bonds. When done, you will have the
enzyme / products complex.
4. The enzyme releases the product.
When the enzyme lets go, it returns to its original shape. It is
then ready to work on another molecule of substrate.
Factors Affecting Catalytic Activity of Enzymes
1. Temperature
This increases the chances of a successful collision and so the
rate increases. There is a certain temperature at which an enzyme's
catalytic activity is at its greatest. This optimal temperature is usually
around human body temperature (37 degrees celsius) for the enzymes
in human cells.
2. pH
The changes in pH can make and break intra- and intermolecular
bonds, changing the shape of the enzyme and, therefore, its
effectiveness.
3. Concentration of Enzyme and Substrate
The rate of an enzyme-catalysed reaction depends on the
concentrations of enzyme and substrate. As the concentration of either
is increased the rate of reaction increases.
4. Inhibition of enzyme activity
Some substances reduce or even stop the catalytic activity of
enzymes in biochemical reactions. They block or distort the active site.
These chemicals are called inhibitors, because they inhibit reaction.