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Caught in the act: The dynamic dance of enzymes
Date:12/11/2007

d strategy that would capture not only the motion of a key protein, but its structures, as well. She had to make sure that the fleeting, more infrequent shapes of enzymes couldnt essentially wiggle out of the picture. These rarer enzyme states are critical to understand, as they are the ones most relevant to better drug design.

Ultimately, Kern harnessed five different elegant techniques, including X-ray crystallography, (NMR), single-molecule fluorescence resonance energy transfer (FRET), computer simulations of molecular dynamics, and paramagnetism, to reveal the full picture of how proteins fold in those infrequent, yet lightening-fast intermediate states between inactivity and activity. Each technique provided a piece of the puzzle.

The big goal here is to understand proteins well enough so that we can actually predict how they will behave, said Kern. These short-lived structures are most likely to have a higher affinity to drug molecules. Instead of relying on trial and error, scientists may be able to rationally design drugs to specifically bind to these intermediate conformations, according to Kern.

With the ability to capture an enzyme in real time as it is moving toward the active state, Kern and co-workers were able to detect picosecond (one millionth of one millionth of a second) changes, the fast smaller conformational motions, as well as the millisecond large-scale motions that are a result of the many fast motions.

This work will lead to understanding the physical nature of proteins not as a static picture but as an ensemble of structures, said Kern.


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Contact: Laura Gardner
gardner@brandeis.edu
781-736-4204
Brandeis University
Source:Eurekalert

Page: 1 2

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