New modeling shows how synonymous mutations—those that change the DNA sequence of a gene but not the sequence of the encoded protein—can still impact protein production and function. A team of researchers led by Penn State chemists modeled how genetic changes that alter the speed of protein synthesis, but not the sequence of amino acids that comprise the protein, can lead to misfolding that changes the protein's activity level, and then corroborated their models experimentally. The results demonstrate the importance of kinetics—the rate of protein synthesis—in addition to sequence for determining protein structure and function and could have implications in fields such as biopharmaceutics for fine tuning the activity of synthesized proteins.
