The formation of macromolecules is a vital process in biological systems, largely driven by the polymerization of monomeric subunits. One such type of macromolecule is a protein, which is composed of amino acids linked together by peptide bonds. Each amino acid contains an amino group, a carboxyl group, and a unique side chain (denoted as R). The specificity of protein function is heavily influenced by the sequence of these amino acids, as well as their three-dimensional structure, which is maintained through various interactions, including hydrogen bonding, ionic interactions, hydrophobic interactions, and disulfide bridges.
Consider the structure of L-sarcosine, a non-proteinogenic amino acid that may play roles in various biochemical pathways. The basic structure is similar to glycine, but L-sarcosine has a methyl group (-CH3) in place of one of glycine's hydrogen atoms. Understanding such modifications to amino acid structure can provide insight into their function and interactions within proteins.
Given this information, which of the following statements accurately describes how a change in the side chain of an amino acid, such as that from glycine to L-sarcosine, can potentially affect protein structure and function?