Biological molecules

proteins
 protein
• Proteins are very important molecules in living
organism
• Proteins are large and complex polymer
molecules, made from large chains of amino
acids.
• Proteins have a wide range of biological roles,
including;
protein
 Amino acid
• All amino acids have a central carbon atom
which is bonded to an amine group and a
carboxylic group.
• The third component that is bonded to the
carbon atom is a hydrogen atom.
• The R group represents a side chain from the
central alpha carbon atom, and can be anything
from a simple hydrogen to a more complex ring
structure.
Structure of amino acid
 Amino acid
• The only way in which amino acids differ from
each other is in the remaining R group.
• In other wards all amino acid have different R
group.
• There are about 20 different types of amino
acids.
Different types of amino acids
 What are Peptide bond
• When two amino acids join together, one
loses (–OH) FROM THE CARBOXYLIC acid
group, while the other loses a hydrogen atom
from its amine group.
• The carbon atom of the first amino acid bonds
with the nitrogen atom of the second.
• The link form is call peptide bond.
Peptide bond
 polypeptides
• Polypeptides are formed when more amino
acids are added to a dipeptide.
• A protein consist of one or more polypeptide
chains folded into a highly specific 3 D shape
polypeptides
• There are four levels of structure in protein.
they include ;
• Primary , secondary, tertiary, quaternary
• Each of these played role in the overall
structure of protein.
 Primary structure
polypeptide or protein containing several hundreds
of amino acids linked into a long chain
The particular amino acid in the chain and the
sequence in which they are joined is called
primary structure of protein.
If a single amino acid is in correct the whole protein
can be useless.
Note; primary structure is the sequence of amino
acids in a polypeptide or protein.
Primary structure
 Secondary structure
• Amino acids in polypeptide chain have an effect on each other
• This polypeptide chain may coil into a cork screw shape called
alpha helix.(secondary structure).
• The secondary structure (alpha helix) is due to hydrogen bonding
between the oxygen of the –co- group of one amino acid and
the hydrogen of the –NH- group of the amino acid four places
ahead of it.
• Some times the hydrogen bonding can result in a much looser,
straighter shape than alpha helix, which is called BETTA pleated
sheet
• Hydrogen bond can be broken by high temperature and pH
changes.
 Secondary structure
• Note : secondary structure is the structure of a
protein molecule resulting from the regular
coiling or folding of the chain of amino acids,
e.g. an alpha or beta pleated sheet
 Tertiary structure
• Tertiary structure is the compact structure of a
protein molecule resulting from the three-
dimensional coiling of the already-folded
chain of amino acids.
• Secondary structure is coiled or folded and
tertiary structure protein coil up to form a
three dimensional shape
Tertiary structure
 Bonds that helps keep folded protein in
their precise shapes
• Hydrogen bonds: form between a wide variety
of R groups.
• Disulfide bond: form between two cysteine
molecules, which contain sulfur atoms
• Ionic bond: form between two R groups
containing amine and carboxylic groups
• Hydrophobic interactions: occur between R
groups which are non polar or hydrophobic
 Quaternary structure
• In most cases protein molecules may have two
or more polypeptide chains.
• Haemoglobin is an example of this, having
four polypeptide chains in each molecule
• The association of different polypeptide chain
is called quaternary structure.
Fibrous proteins
 Globular protein
• A protein whose molecules curl up into a ball
shape is known as golbular
• E.g. myoglobin , haemoglobin.
• Globular proteins usually curl up so that their
non- polar, hydrophobic R group point into the
centre of the molecule, away from their
watery surroundings
Globular Proteins
Denaturing protein