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PROTEIN DENATURATION

The familiar gelatin dessert actually is a good example of the process of coagulation of
proteins into a 3-dimensional latticework that entraps water molecules to produce a
semisolid gel.

Protein denaturation changes the solubility of individual protein molecules,entrapping


solvent water into a semisolid gel structure.Protein are synthesized by polymerizing
amino acids.The polymerization occurs by repeatedly forming peptide bonds that link
individual amino acids together into a chain. There are 3 structural features that influence
the three-dimensional shape of water-soluble protein.

Primary structure is the peptide bond between individual amino acids that creates a
long chain of connected amino acids.These long chains of polymerized amino acids have
hydrophobic(water repelling) and hydrophilic(water attracting) projections that are
oriented perpendicular to the chain.

Secondary structure is the helix that the protein chain curls into,as a result of hydrogen
bonds and other weak forces.

Tertiary structures is created when the protein molecules fold back on themselves
outside of the helical segments,to put the hydrophobic portions to the interior and the
hydrophilic portions to the exterior.

Several helix regions can exist in different portions of the molecules.When the protein
has folded and refolded to reach its most stable configurations,it will have mostly
hydrophilic amino acid residues on the exterior,and mostly hydrophobic residues directed
into the interior.

When natural proteins are subjected to physical or chemical treatment,their structure


changes,and they become ‘un-native’ or ‘un-natural’.We call that process denaturation.
In this example,heating the proteins in solution imparts energy to the protein
molecules.This added energy is enough to break the relatively weak forces that hold the
protein in its refolded and helical tertiary and secondary configurations.As the process of
denaturation proceeds,the protein molecule unfolds more and more and internally
directed hydrophobic regions now become exposed on the outside of the molecule.

The peptide bonds are largely hydrophilic.Once these segments are set from each
other,they attract water molecules.The recruitment of water molecules entraps the water
molecules in close proximity to the protein strands. The hydrophobic portions of the
molecules are also exposed.This situation is unfavored because the hydrophobic portions
of molecules are not stable in an aqueous environment.Hence,upon unfolding,the
hydrophobic regions on individual protein molecules will associate with hydrophobic
regions on other protein molecules.
This situation encourages the association of these protein molecules into larger and
larger random 3-dimensional structures.The molecules aggregate into very large,water-
insoluble collections that are quite randomly assembled.

As the proteins denature,lattice-work structure grow amorphously and attract the solvent
water molecules into cell-like structures.

The self associated water molecules,in groups,adhere t the surface of hydrophilic


regions of the protein while hydrophobic regions of the protein dissolve into each other
and provide the energy to retain the structure.

As this process continues irreversibly,all of the protein molecules are recruited to this
large insoluble mass in randomly organized structural framework that contains entrapped
water molecules.

One example of the consequences of unfolding and re-associating protein molecules is


coagulation of egg white.Frying an egg is no more complicated than denaturing the egg
white protein.

The assembly of irreversibly denatured protein molecules results in formation of solid


gel.The gel entraps water molecules inside the white into a semi-solid structure,which
holds its shape under normal conditions.

Other examples of denatured protein assembling into three-dimensional structures


include the baking of yeast-risen bread,coagulation of meat proteins by cooking in such
products as hot dogs,and in the solidification of gelatin cooling of a solution.

Denaturation and coagulation of protein is a complex,irreversible process but the study


of denaturation has allowed to us to better understand the three-dimensional structure of
native proteins.

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