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.

One example of the consequences of unfolding and re-associating protein molecules is coagulation of egg white. Other examples of denatured protein assembling into three-dimensional structures include the baking of yeast-risen groups.Frying an egg is no more complicated than denaturing the egg white protein.lattice-work structure grow amorphously and attract the solvent water molecules into cell-like structures.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.and in the solidification of gelatin cooling of a solution. .waterinsoluble collections that are quite randomly assembled.all of the protein molecules are recruited to this large insoluble mass in randomly organized structural framework that contains entrapped water molecules. Denaturation and coagulation of protein is a complex.The molecules aggregate into very large. As this process continues irreversibly.which holds its shape under normal conditions. The self associated water molecules.The gel entraps water molecules inside the white into a semi-solid structure. The assembly of irreversibly denatured protein molecules results in formation of solid gel.irreversible process but the study of denaturation has allowed to us to better understand the three-dimensional structure of native proteins.coagulation of meat proteins by cooking in such products as hot dogs.This situation encourages the association of these protein molecules into larger and larger random 3-dimensional structures. As the proteins denature.

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