Interface mutants of glyoxysomal malate dehydrogenase

Biochemical studies are becoming increasingly more interesting and beneficial since the human genome project in which the covalent structure of proteins was discovered. Projects such as that one lay the groundwork for complex studies into the function and dynamics of proteins. Protein folding, catalysis, inhibition and activation, among other things are all controlled by the non-covalent relationships among the amino acid residues that comprise the protein and its environment. We\u27 re interested in studying a protein present in many isoforms that displays unique function under varying conditions. Therefore the protein that we chose to study is malate dehydrogenase (Figure 1)