When a protein enters the low-pH environment of the stomach, charges on amino acid side chains are changed. These changes break ionic bonds, which changes the structure of the protein. This will change the:

a) Secondary structure of the protein.

b) Amount of buffer in the stomach.

c) Function of the protein.

d) Primary structure of the protein.

Large monomer chains form biological macromolecules that perform many essential body functions, including nucleic acids, carbohydrates, proteins, and lipids. These are organic molecules, meaning Carbons bonded to the elements oxygen (O), hydrogen (H), nitrogen (N), and phosphorus (P) are ringed or long-chain.

Proteins are structural support molecules consisting of long amino acid chains joined by peptide (CONH) bonds; these are 20 different units organized into several macromolecules. Amino acids are absorbed through digestion and incorporated into the cells of the body to form muscle organs that signal molecules and provide an alternative source of energy.

Higher order protein structure, or how a protein folds, is influenced by hydrogen bonding and side chain interactions. pH changes can directly affect and hinder folding, how proteins are shaped and by extension, their function.

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