Using lasers to initiate and probe the folding process, a group including chemist Timothy Zwier have precisely determined the energies needed to twist tryptamine, a molecule with several flexible "hinges" that bears a close resemblance to an amino acid, the basis of proteins. Understanding the energy pathways that these molecules take passing from one conformation to another could provide new understanding of the elusive process of protein folding - an essential part of the development of these fundamental biological molecules. And though tryptamine forms only a tiny portion of a protein, a better understanding of this close chemical relative to serotonin and melatonin could provide insights into these other substances' effect on the brain.

"If you want to know how molecules function in the body, you can't just look at their structure - you have to look at the dynamics of how they change," said Zwier, who is a professor of chemistry in Purdue's School of Science. "On a small scale, we have found a way to look at the dynamic processes that makes one such molecule change shape. While we're still a long way from understanding how proteins take on their complex shapes, this work could be a step in that direction."

This research, which Zwier conducted with graduate student Jasper Clarkson and former student Brian Dian (now a postdoctoral researcher at the University of Virginia), appears in the current (Feb. 20) issue of the journal Science.

For the past several years, science magazines have regularly adorned their covers with intricate, multicolored spirals - illustrations that represent the recently revealed internal structure of proteins, some of the most complex molecules known. To atta
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Contact: Chad Boutin
cboutin@purdue.edu
765-494-2081
Purdue University
25-Feb-2004