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BIOLOGICAL IMPORTANT OF MOLECULAR

CHAPERONES IN PROTEIN FOLDING

Molecular chaperones are a group of unrelated protein families whose role is to


stabilize unfolded proteins and assist in their correct folding and assembly. Molecular
chaperones are essential for protein folding and they are encoded in the primary
sequence as the N-terminal or C-terminal extension.

Protein folding is the process by which a protein structure assumes its functional
shape. Proteins are able to perform their biological functions by coiling and folding
into a specific three dimensional shape.

Molecular chaperones consist of highly conserved families of proteins, many of


which consist of heat stock proteins. The primary function of molecular chaperones
is to facilitate the folding of protein and they also play an important role in cellular
processes such as protein synthesis, protein translocation and degradation of protein
after cell stress. Molecular chaperones are classified into two types: type 1 and type
2.
The type 1- mediates the folding protein into their respective tertiary structure and
mostly produced as the N-terminal sequence.

The second type mediates the formation of the functional structure of the protein
and usually located at the C-terminal of the protein.

Molecular chaperones are important in protein folding in the following ways:

Prevent inappropriate association or aggregation of exposed hydrophobic


surfaces and direct their substrates into degradation pathways.
Stabilize non-native conformation and facilitate the correct folding of protein
subunits.
They act as a catalyst, they facilitate the assembly without being part of the
assembled complex.
They bind and stabilize unfolded polypeptide along the pathway leading to the
correctly folded state.
During folding chaperones bind to the N-terminal of the growing polypeptide
chain, stabilizing it in an unfolded configuration until the synthesis of
polypeptide is completed.
Some molecular chaperones are hydrolysis of folding process and form the
part of the final folded structure.
Molecular chaperones are divided into protein families, namely Hsp70 and Hsp60.
These proteins families prevent aggregation of newly synthesised polypeptides and
then mediate their folding to the native state.

Hsp70 is a simple chaperone that is found in all living organisms, It function is to


protects unfolded protein. It also plays many roles in the cell. It guides protein across
the membrane. It has N-terminal domain and C-terminal region which is a substrate
binding domain. Hsp70 can only bind unfolded protein by recognizing an extended
region of a polypeptide chain that is rich in hydrophobic residues. Therefore the
chain containing many hydrophobic amino acids can only be burned by hsp70,
except compact globular proteins that contains hydrophilic amino acids on their
surface. Unfolded proteins can be clumped by several hsp70 molecules to prevent
aggregation.

Hsp60 is a molecular chaperone that functions to isolate unfolded protein and


provide the optimal environment for on pathway folding. It also promotes proper
folding. They provide isolation chamber in which individual unfolded protein can fold.
Hydrophilic environment favours the burial of hydrophobic amino acids in the
substrate and exposure of hydrophilic on their surfaces, thus proper folding is
promoted.

The most important function of molecular chaperone is to aid in the proper folding of
proteins. The protein folding can be affected by factors such as PH and heat of the
cell, which can result in an aggregation or misfolding of proteins. The failure of
protein folding can be the result of an absence of cofactors called molecular
chaperones and factors mentioned above.

REFERENCES

Www. Google.com

www.researchgate.snet

C B Anfinsen principles that given the folding of proteins chains, science 181- 1973
223-238

Hartl, F.U. and Hayer-Hartl, M. (2002) molecular chaperones in the cytosol: from
Nascent chain to folded protein. Science 295,1852-1858

Articles based on protein folding.