Page 101 - The Miracle of Protein

ADNAN OKTAR (HARUN YAHYA) 99

Chaperone Proteins

Molecules that play a part in folding are called chaperone
proteins. In order for the proteins to be active in the cells, they
require the correct three-dimensional structure. When the
amino acids fold onto themselves, the proteins attain their 3D
structure. However, even the slightest mistake in this three-di-
mensional structure will make the protein lose its functions.
Researchers previously thought that proteins folded cor-

rectly by themselves, due to their amino acid sequences. How-
ever, it was later revealed that chaperone proteins were respon-
sible.
The reference text book Genetic Concepts summarizes this
interesting detail about the proteins:

“In order for a protein to obtain its unique function, the afore-
mentioned post-translation changes (the phase after the pro-
tein is produced in ribosome) are very important. Since the
three-dimensional structures of the proteins determine their
functions, how the polypeptides fold to assume their final con-
formation is critical. For years, researchers believed that pro-
tein folding was a spontaneous action that would ensure max-
imum thermo-dynamical resistance and that it depended on
the sum of the chemical qualities of the amino acids in the
polypeptide chain. However, research have shown that ele-
ments of the ubiquitin family (a protein family that can be
found in every cell), named chaperones played a major role in
the folding of many proteins. The mechanisms of chaperones
aren’t fully uncovered yet. These molecules emerge from their
reactions without any change, just like enzymes. Chaperones
were first discovered in drosophila and were originally named
heat-shock proteins. Later, it was found that they were also pre-
sent in various organisms including bacteria, animals and

plants.” 30