Cysteine Residues in Receptor Proteins： Structural Insights from Two E. coil Periplasmic Binding Proteins

Cysteine residues found in proteins have various functions such as metal binding, nitrosylation, and stabilization of structure. We have done a comparative, computational structural analysis of the cysteine residues in two proteins from bacteria to get some insight into the differences between metal binding cysteine residues and those involved in structure stabilization. The two target proteins in this study are the periplasmic mercury binding protein （MerP） and the 1-1eucine binding protein （LBP）. Both are periplasmic binding proteins from E. coli. We have shown key phenomenon that define cysteines as metal binding or structural in nature.