University of Wisconsin-Madison researchers said the first applications of their technique focused on the protein hIAPP, believed involved in type 2 diabetes.

Although scientists have a good idea of the healthy "before" and dangerous "after" hIAPP structures, the steps between remain somewhat of a mystery.

"We need tools that not only allow us to probe the molecular structures but also look at how the structures change in time," said Professor Martin Zanni, the study's leader.

A few years ago, Zanni's team built the first device capable of designing infrared laser beams with a computer. The team has refined the process, obtaining a single structural scan of hIAPP in less than a second -- more than 500 times faster than previously possible.

The group now plans to capture series of snapshots during individual folding reactions.

"No matter how fast they're moving, we can take pictures of them," said Zanni.

The technology is described in the online issue of the Proceedings of the National Academy of Sciences.