As the protein moves to a lower pH region, its surface charge will become less negative, and a pH region will be reached at which the protein net charge is zero (the isoelectric point).

Explanation: In a globular protein, the amino acid chain can twist in a way that polar groups lie at the protein’s surface. This allows the protein to interact with water and enhances the protein’s solubility in water. This does not occur in fibrous proteins, so fibrous proteins are insoluble in water.

Changes in pH affect the chemistry of amino acid residues and can lead to denaturation. Protonation of the amino acid residues (when an acidic proton H + attaches to a lone pair of electrons on a nitrogen) changes whether or not they participate in hydrogen bonding, so a change in the pH can denature a protein.

If the protein is subject to changes in temperature, pH, or exposure to chemicals, the internal interactions between the protein’s amino acids can be altered, which in turn may alter the shape of the protein. the enzyme that breaks down protein in the stomach, only operates at a very low pH.

Proteins are denatured by treatment with alkaline or acid, oxidizing or reducing agents, and certain organic solvents. Interesting among denaturing agents are those that affect the secondary and tertiary structure without affecting the primary structure.

Temperature, pH, salinity, polarity of solvent – these are some of the factors that influence the shape of a protein. If any one or combination of these factors varies from normal conditions the shape (and function) of the protein will change. This change in shape is also called denatured.

Changes in pH, Increased Temperature, Exposure to UV light/radiation (dissociation of H bonds), Protonation amino acid residues, High salt concentrations are the main factors that cause a protein to denature.

Pepsin, the enzyme that breaks down protein in the stomach, only operates at a very low pH. At higher pHs pepsin’s conformation, the way its polypeptide chain is folded up in three dimensions, begins to change. The stomach maintains a very low pH to ensure that pepsin continues to digest protein and does not denature.

High temperature weakens the inherent bonds in protein. However, at very high salt concentration, the increased surface tension of water generates a competition between protein and salt ions for hydration. Salts strip off the essential layer of water molecules from the protein surface eventually denaturing the protein.

Since a protein’s function is dependent on its shape, a denatured protein is no longer functional. It is not biologically active, and cannot perform its natural function.

If the protein denatures, your body won’t be able to absorb it!”

When a protein is denatured, secondary and tertiary structures are altered but the peptide bonds of the primary structure between the amino acids are left intact. Since all structural levels of the protein determine its function, the protein can no longer perform its function once it has been denatured.

Enzymes have specific functions in the body, such as working to break down food or causing other chemical processes. Enzymes never die, but they are not considered to be either living or nonliving organisms. When enzymes denature, they are no longer active and cannot function.

Higher temperatures disrupt the shape of the active site, which will reduce its activity, or prevent it from working. The enzyme will have been denatured . The enzyme, including its active site, will change shape and the substrate no longer fit. The rate of reaction will be affected, or the reaction will stop.

As the temperature rises, reacting molecules have more and more kinetic energy. Above this temperature the enzyme structure begins to break down (denature) since at higher temperatures intra- and intermolecular bonds are broken as the enzyme molecules gain even more kinetic energy.