Investigating the Function of Disulfide Bonds in Proteins with Molecular Dynamics Simulations

Disulfide bonds are covalent bonds formed by the oxidation of cysteine side-chains and are present in at least 20% of proteins, but their function is not fully understood. In our study, we primarily use molecular dynamics simulations to analyze their role in stability and activity. Using three different proteins(RNase, LTP and HVEM) as examples, we will discuss the methods and ways to analyze the obtained data.