PROTEIN

Folding

Misfolding

When two amino acids are joined together, the bond formed is called a
peptide bond.
Sickled red blood

When the environment changes

(i.e. increased heat or changes
in pH), proteins can unfold or
Denature. This loss of three
dimensional shapes will usually
be accompanied by a loss of
proteins functions. If the
denatured protein is allowed to
cool, itll sometimes refold
back
into
its
original
conformation.

A normal CFTR
protein regulates the
amount of chloride
ions across the cell
membrane of lung.
If too salty, water is
drawn from lung
mucus by osmosis.
CFTR gene are
mutated.

Proteins Structure :
1. Primary

The sequence of amino acids in the

The
sequence chain.
of amino
in the
chain. The
polypeptide
The acids
sequence
of polypeptide
R
2. Secondary
sequence
of R groupsthe
determines
the of
properties
of the proteins. A
groups determines
properties
the
change
of single
amino
acid can
alteracid
the function
of the proteins.
proteins.
A change
of single
amino
can
Example
:
alter the function
of the proteins.
Sickle cell anemia caused by a change one amino acid from
Example :
glutamine to valine.
anemia caused by a change
Folding and coiling due to HSickle
bondcell
formation
one
amino
acid
from glutamine
3. Tertiaryto valine.
between carboxyl and amino groups of nonadjacent amino acid, R groups are NOT involved.
Two common examples are the alpha helix and the
beta pleated sheet.

2. Secondary

and

The 3-D structure resulting from folding of 20

structural elements. Stabilized by bonds formed
between amino acid R groups. Forms many
shapes, such as globular compact proteins and
fibrous elongated proteins.
4. Quaternary

Relationship among multiple polypeptide chains forming a protein. 3-D structure due to interactions between polypeptide chains. R- group