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Researchers find 'north pole' of the molecular world

Researchers have devised a method to determine the alignment of a molecule's axis, the "poles" that govern how a molecule will interact with others. The advancement will help scientists and engineers predict the ways that atoms and molecules exchange energy, possibly enhancing solar energy devices or helping biochemists better understand proteins. The research, appearing in the June 4 issue of Physical Review Letters, shows how a tightly-focused laser employing a new kind of polarization can produce valuable images of individual molecules in three dimensions.

The new method takes a snapshot of a phenomenon called the "molecular dipole moment." This "moment" is an axis that runs through the molecule like a north and south pole, along which energy is emitted and absorbed. If two molecules are positioned so that their respective poles align, they are more likely to exchange energy. If they are completely misaligned, then an interaction is more difficult. Someday, researchers hope to control the alignment to direct chemical reactions at the atomic level.

"By imaging the dipole movement of certain molecules we can see exactly how certain chemical reactions happen," says Lukas Novotny, assistant professor of optics at the University of Rochester. "Were working now with biochemists to understand how various proteins in the body form."

Proteins fold when they form, but monitoring their folding is a tricky business that the Rochester teams method can help clarify. To watch the folding process, researchers place two marker molecules at each end of the proteinone marker emits green light when stimulated, and the other emits red. One marker (the green one) is charged with energy so that it emits its light. When the protein folds itself and brings these two markers together like a gymnast touching her toes, the green marker gives some of its energy to the other, which then glows, causing a change in the overall color of light emitted from the protein. Exactly whe
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Contact: Jonathan Sherwood
jsherwood@admin.rochester.edu
716-273-4726
University of Rochester
3-Jun-2001


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