Proteins are vastly more complicated than previously realized

ison of the early stages of forced unfolding for fibronectin type III modules" appears in the May 1 Proceedings of the National Academy of Science, a journal of the National Academy of Sciences.

Fibronectin is a useful protein for studying the effects of mechanical force. Fibronectin is found in connective tissue, such as the skin. In the skin, cells are suspended in the extracellular matrix consisting of thousands of protein fibers that attach to cells at numerous points. These proteins connect with other proteins and hold the mass together a sort of super glue for cells. It is the movement of these fibers and the resulting pull and push on the cells attached to them, that transmits force to the cells.

Vogel and colleagues ask these questions: What does force do to the fiber? How is force transmitted from the fiber to the cell? And how is force used to determine how the cell regulates the expression of certain proteins? "We are very excited about this because we believe a new field is being born: non-equilibrium protein structure-function analysis. Its very exciting to think about how nature regulates and controls function. We went from viewing the cell as a bag full of proteins a decade ago to a view of the cell as a dynamic place where proteins assemble and change under mechanical forces," Vogel says.

This new field became possible only in 1997, with the technology that allowed researchers to see what happens when you grab either end of a protein and stretch, using tools such as atomic-force microscopy. They found that proteins rupture as stretching forces overcome energy barriers that stabilize the protein structure.

"Computer simulations allow us to see what happens to the structure if the protein ruptures," Vogel says. The computer simulations were done in collaboration with Dr. Klaus Schulten at the Beckman Institute in Illinois and former UW graduate student Andre Krammer. "People tend to think of protein function as biochemical che

Contact: Walter Neary
University of Washington

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