Divalent metal cations support the folding of metalloproteins

WCC 14

Elita Pastra-Landis, Department of Chemistry, Wheaton College, Norton, MA 02766
Research at an undergraduate liberal arts college poses unique challenges and commensurate rewards. Five decades ago, Bojan Jennings did this successfully by teaching successive generations of students to work together. The accumulation of experimental results generates new answers leading to publications. It also demonstrates that science progresses best when shared collaboratively. Having followed Bojan's advice and path to join the faculty at Wheaton College, I emulate her approach to research. The contributions of a number of students over some years lead to new knowledge in the field. I will discuss recent examples of such work. In particular, we have investigated the influence of divalent metal ions on the folding strength of the enzyme Alkaline Phosphatase from E. coli. The native metal ions, two zinc and one magnesium, are coordinated at the active site, providing not only the functional basis of catalysis, but also extraordinary structural stability for the three-dimensional fold.