Purdue scientists have made an important biological molecule "swing," in work that might clarify the process by which proteins fold as well as lead to new approaches to drug development and computer memory.
This metaphorical "mountain range" of peaks and valleys represents the different energy states which can be assumed by a tryptamine molecule, closely related to the brain-influencing substances serotonin and melatonin. A single tryptamine molecule can have several different configurations depending on how much energy it has received, and tends to stay in one configuration – represented by the red "valleys" on the chart – until enough energy is added to make it climb out of the valley and cross the range to another steady energy state. Tim Zwiers group at Purdue University has used lasers to explore the precise energies required to move a molecule from one valley to another, making it far easier to determine the route tryptamine takes as it changes configuration. The work could impact the study of how proteins fold and could lead to new approaches to develop computer memory devices. (Purdue illustration/Timothy Zwier)
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 cant 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 Purdues 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 were still a long way from understanding how proteins take on their complex shapes, this work could be a step in that direction."
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