Metalloprotein Program Project Overview
One-third of all proteins are "metalloproteins", chemical combinations of protein atoms (carbon, nitrogen, oxygen, hydrogen, sulfur) with ions of metals such as iron, calcium, copper, and zinc. The hemoglobin, for example, that carries oxygen in the bloodstream, is an iron-containing metalloprotein. The metal ions in metalloproteins are critical to the protein's function, structure, or stability. In fact, numerous essential biological functions require metal ions, and most of these metal ion functions involve metalloproteins. Thus, metalloproteins make life on Earth possible and the ability to understand and ultimately control the binding and activity of protein metal sites is of great biological and medical importance.
Over the next five years, this Program aims to overcome current problems
relating metalloprotein structure and function. Our major focus is to establish
a direct experimental correlation between structural design parameters and
metalloprotein properties by using an accurate database of protein metal
sites, explicit evaluation of possible states, projects that separate general
and framework-specific effects, and efficient computational searches in the
vast combinatorial landscape of the metal site environment. The ultimate
goal of our research is to achieve a comprehensive understanding and the
successful design of metalloproteins.
For More
Info: Judy Palmer
(judyp@scripps.edu)
NEW!
Images from the November 2000 retreat (off-site at the moment)