Proteins play a host of indispensable roles. There are enzymatic proteins that catalyze the chemical reactions in cells—thousands of different enzymes sparking thousands of different critical reactions. There are transport proteins, such as the hemoglobin responsible for carrying iron through the blood. Collagen and elastin provide structure, while other proteins are responsible for muscle movement. Some proteins store amino acids to nurture developing embryos and baby mammals. Hormonal proteins, like insulin, coordinate the body’s essential functions, while receptor proteins in the membranes of nerve cells detect chemical stimuli. And defensive proteins fight disease-causing bacteria and viruses.
In order to better understand these processes, biologists need to better understand the underlying proteins. That understanding could help researchers craft therapies to combat diseases caused by missing or malfunctioning proteins.To understand a proteins function, you must know its structure.
Proteins are strings of amino acids, but these strings are folded and tangled into complex three-dimensional structures; the unique structure of each protein allows it to function in a unique way. Currently the standard techniques for determining protein structure are X-ray crystallography and nuclear magnetic resonance, but these techniques are time-consuming and therefore ill-suited to determining the structures of the hundreds of thousands of proteins of interest to scientists. Some proteins cannot be crystallized at all. And according to University of Washington researcher David Baker these processes can be a difficult and tedious. To reduce the difficulty, relieve the tedium, and realize costs savings, Baker is working to develop another method, one that relies on computation rather than experimentation.