STRUCTURAL ORGANISATION OF PROTEIN

at different levels and their clinical significance

ROOL NO. 116-120
 WHAT IS PROTEIN?
proteins are macromolecule composed of one or more polypeptide chains
each with a characteristic sequence of amino acid linked by peptide bonds

To perform their biological functions. Protein fold into one or more

specific spatial arrangement at different levels
LEVELS OF ORGANISATION
1 Primary structure of protein

2 Secondary structure of protein

3 Tertiary structure of protein

4 Quaternary structure of protein

 PRIMARY
STRUCTURE OF
PROTEIN
The Primary structure of protein
Theystructure
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Under the microscope, the most evident
part of the cell is the nucleus. It is also
Secondary structure is maintained by hydrogen
the most crucial part of it.
bonds between amide hydrogens and carbonyl
oxygens of the peptide backbone.
SECONDARY
STRUCTURE OF
PROTEIN
The folding of polypeptide chains into regular
or ordered structure by repetitive hydrogen
bonds between NH and CO groups of the
peptide bonds of amino acid is called
secondary structure.
 TYPES OF SECONDARY STRUCTURE OCTOBER 2030

1. ALPHA HELIX

2. BETA PLEATED SHEET

 Alpha helix
1. In this structure, the polypeptide backbone is tightly wound in the
fashion of a spring around an imaginary axis drawn longitudinally
through the middle of the helix and the R groups of the amino acids
residues protrude outward from the helical backbone.
2. All alpha helix found in proteins are right-handed
3. About 75% of residues in ferritin ,a protein that stores iron, are in alpha
helices.
4. About 25% of all soluble proteins are composed of alpha helices.
5. Alpha helical structures are stabilized by intramolecular hydrogen
bonding
 Beta pleated sheet structure

1. In the beta -conformation, the backbone of the polypeptide chain is

extended into a zigzag pattern rather than helical structure.
2. These structures is stabilized by intermolecular hydrogen bonding.
3. The adjacent polypeptide chains in beta sheet can be either parallel or
anti-paral.
4. In parallel structure adjacent chains aligned in same direction whereas
in antiparallel sheet structure ,the alignment are in opposite direction.
5. Proteins containing beta sheet structures are:
1. Fatty acid-binding proteins are made almost entirely from beta sheets.
2.A protein transthyretin also contain beta structures.
3.Silk fibroin also contain beta sheet structures.
 Tertiary structures of protein
1. The overall three dimensional arrangement of all atoms in a protein is referred to as the protein
tertiary structure 'or 'the secondary structures is further folded and twisted about itself in such
a way as to achieve maximum stability forming the three dimensional structures.
2. In tertiary structures domains are present.
3. A domain is a section of a protein structure, sufficient to perform a particular chemical or
physical function.
4. Tertiary structures of proteins are stabilized by following:
Hydrogen bond
hydrophobic interactions
Van der waals forces
disulfide bond
ionic bond or salt bridges
5. Example -- myoglobin
 Quaternary structure of protein
1. Proteins that have more than one polypeptide chain in their native conformation have
quaternary structure.
2. The arrangement of these polypeptide subunits in three- dimensional complexes is called
quaternary structure of the protein.
3. Example -- hemoglobin
4. Quaternary structures are stabilized by: hydrophobic interactions, hydrogen bond, ionic bonds
and disulfide bonds.
5. In quaternity structures polymeric proteins may either function independently of each other
or may work cooperatively.
 CLINICAL SIGNIFICANCE

1. PROTEIN 2.DENATURATION
MISFOLDING OF PROTEIN
PROTEIN MISFOLDING
Misfolded protein occur when a protein follows the wrong folding pathway
Causes of protein misfolding
a.Genetic mutation
b.translation or transcription error
c. environmental stress
d. post transitional modification and other factors
Result of protein misfolding
1.Alzheimer's disease
2.Parkinson's disease
3.huntington's disease
DENATURATION OF PROTEIN
Denaturation is the process by which protein loses its secondary tertiary and
quaternary structure.
It occurs when a proteins weak bond like hydrogen bonds are broken. This
breaks the protein's highly ordered structure into a looser more random
structure.
Denatured proteins are no longer functional because their function depends on
shape.
Factors inducing denaturation
Heating, treatment with alkaline, acid urea, high salt concentration, alcohol,
mechanical agitation