1) Protein:

- Chains of amino acids molecules connected by peptide bonds

2) General structure of an amino acid:






3) Primary Protein:
- The sequence of amino acids in the polypeptide chain with reference to
the locations of any disulfide bonds.
- For example:
gly-gly-ser-ala is the primary structure for a polypeptide composed
of glycine, glycine, serine, and alanine, in that order, from the N-terminal
amino acid (glycine) to the C-terminal amino acid (alanine).

4) Secondary protein:
- The ordered arrangement of amino acids in localized regions of a
polypeptide or protein molecule.
- The two main secondary structures are the alpha helix and the anti-
parallel beta-pleated sheet.
- Hydrogen bonding plays an important role in stabilizing these folding
patterns.



5) Tertiary protein:
- The three-dimensional arrangement of the atoms within a single
polypeptide chain.
- Tertiary structure is largely maintained by disulfide bonds (Disulfide bonds
are formed between the side chains of cysteine by oxidation of two thiol
groups (SH) to form a disulfide bond (S-S))

6) Enzyme:
- Proteins that catalyze biochemical reactions
- They increase the rate of a reaction but are not used up in the process.
- Enzymes are able to catalyse reactions in aqueous solutions under
exceptionally mild conditions of temperature and pH.

7) Catalysis:

Substrate (key)
Active site

Enzyme (lock)

- Only specific substrate (key) can fit into the active site of the enzyme.
- The appropriate substrate (key) will bind to the active site of the enzyme
to form an enzyme-substrate complex.
- Enzyme-substrate complex then undergoes a conformational change
(Induced fit) that converts the substrate(s) into product(s).





8) Denaturation:
- The change in the three-dimensional structure of an enzyme caused by
temperature and pH value of its surroundings.
- The high/low temperature and high/low pH disrupts the bonds of the
enzyme, changing its shape. If the shape of the enzyme is denatured or
interrupted, its substrate will no longer fit into it.

9) Competitive inhibition
- The inhibitor acts on the same active site as the normal enzyme substrate.
- The substrate molecules cannot enter the active site while the inhibitor is
there and vice versa.
- The inhibitor does not react with the enzyme; it just gets in the way.
-

10) Non-competitive inhibition
- The inhibitor works by occupying some other site on the enzyme.
- Because of this, the substrate and inhibitor do not compete for access to
the same site.
- Rather, the inhibitor alters the shape of the enzyme in such a way that
prevents the substrate from binding to the enzyme.
- In this mode of inhibition, the activity of the enzyme is completely blocked
by the inhibitor and increasing the concentration of substrate does not
restore enzyme activity.

E + Ic E Ic complex