This is because the bonding brings about tertiary structure and interactions between the R groups determines the compact 3D shape of the globular proteins. The protein / enzyme has been denatured.Īll proteins have tertiary structure which depend on the sequence of amino acids and R groups (determined by) in the primary structure of the polypeptide chain. If the bonds are altered or broken, the shape of the protein / enzyme changes, the characteristics change and the protein / enzyme function changes. This leads to changes in the ionic charges and eventually causes ionic bonds to break.Īll enzymes have a 3D tertiary structure.The function of a protein or an enzyme depends on its particular characteristics, in particular the shape of the protein / enzyme, which is determined by its bonds. Therefore, changing the hydrogen ion concentration of a solution, namely the pH value, alters the charge of amino acids, which in turn interact with any charges on the R groups (of the substrate?).
Alternatively, reducing the hydrogen ion concentration of the solution means the amine group donates hydrogen atoms (ions?) making the overall charge negative. When the hydrogen ion concentration of a solution of an amino acid increases, protons are attracted to the negatively charged carboxyl group and therefore the overall charge becomes positive due to the amine group also being positively charged.
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