PROTEIN

Folding

Misfolding

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

ood cells

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

3. Tertiary
2. Secondary

2. Secondary

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

and
The sequence of amino acids in the
The
sequence of
aminoThe
acidssequence
in the polypeptide
polypeptide
chain.
of R chain. The sequence
ofgroups
R groups
determines
properties of
of the proteins. A change of
determines
thetheproperties
proteins.
A
change
of
single
amino
acid
single amino acid can alter the function ofcan
the proteins.
alter
the
function
of
the
proteins.
Example :
Sickle
cell :anemia caused by a change one amino acid from
Example
glutamine to valine.
Sickle cell anemia caused by a change
Folding and coiling due to H bond formation
one amino acid from glutamine to 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.

Relationship among multiple polypeptide chains

forming a protein. 3-D structure due to interactions
between polypeptide chains. R- group interactions, H
bonds, ionic interactions. Assembled after synthesis.
Only proteins with more than one sub-unit can have
a quaternary structure.