to no significance. However, recent research suggests that such alterations to the triplet code do affect protein translation efficiency and protein folding and function. Furthermore, a change in primary structure is critical because the fully folded tertiary structure of a protein is dependent upon the primary structure. The discovery was made throughout a series of experiments in the 1960s that discovered that reduced and denatured RNase in its unfolded form could refold into the native tertiary form. The tertiary structure of a protein is a fully folded polypeptide chain with all hydrophobic R-groups folded into the interior of the protein to maximize entropy with interactions between secondary structures such as beta sheets and alpha helixes. Since the structure of proteins determines its function, it is critical that a protein be folded correctly into its tertiary form so that the protein will function properly. However, it is important to note that polypeptide chains may differ vastly in primary structure, but be very similar in tertiary structure and protein function. Secondary structure Silent mutations alter the secondary structure of mRNA. Secondary structure of proteins consists of interactions between the atoms of the backbone of a polypeptide chain, excluding the R-groups. One common type of secondary structures is the alpha helix, which is a right-handed helix that results from hydrogen bonds between the nth amino acid residue and the n+4th amino acid residue. The other common type of secondary structure is the beta sheet, which displays a right-handed twist, can be parallel or anti-parallel depending on the direction of the direction of the bonded polypeptides, and consists of hydrogen bonds between the carbonyl and amino groups of the backbone of two polypeptide chains. mRNA has a secondary structure that is not necessarily linear like that of DNA, thus the shape that accompanies complementary bonding in the structure can have significant effects. For example, if the mRNA molecule is relatively unstable, then it can be rapidly degraded by enzymes in the cytoplasm. If the RNA molecule is highly stable, and the complementary bonds are strong and resistant to unpacking prior to translation, then the gene may be under expressed. Codon usage influences mRNA stability. Furthermore, since all organisms contain a slightly different genetic code, their mRNA structures differ slightly as well, however, multiple studies have been conducted that show that all properly folded mRNA structures are dependent on the primary sequence of the polypeptide