Proteins are vastly more complicated than previousl...( The function of proteins the workhor...)

The function of proteins the workhorses of our bodies depends on how those proteins are physically folded. Researchers around the world are examining the countless complex structures of proteins to learn more about therapies for the human body. Protein folding has been compared in complexity to the folding of delicate origami.

This folding process is more complicated than previously realized, according to University of Washington researchers. Imagine trying to fold a delicate origami crane from silk paper while youre in a wind tunnel. In fact, imagine trying to fold the origami in a wind tunnel while countless other hands are also pulling at the paper. And yet, thats comparable in complexity to what the hundreds of thousands of cells and proteins are doing in your body right now.

Thats because proteins and cells are locked together at numerous contact points. The movement of a cell stretches the proteins around it, and vice versa. A new UW study says scientists are going to have to study how protein structures change when stretched before they understand how the body functions.

"The function of a protein is tightly controlled by its structure, yet there is very little information about how mechanical forces may change the structure of proteins," says Dr. Viola Vogel, director of the University of Washingtons Center for Nanotechnology in the Department of Bioengineering. "Right now, it feels like we are only looking at part of the equation of how proteins work since we just know their equilibrium structures. If you do not know how mechanical forces change the function of cells and proteins, you will not understand different diseases that involve mechanical forces, such as hypertension."

Vogel is one of the authors of the first paper to show, at atomic resolution, how mechanical forces change the structure of a family of protein modules that fold into the same structures -- yet have less than 20 percent of their amino acids in common. "Compar
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Contact: Walter Neary
wneary@u.washington.edu
206-685-3841
University of Washington
1-May-2001