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Measuring protein movements with nanosecond resolution
Date:3/15/2010

f the protein responsible for binding actin to fold and unfold on a time scale of 100 nanoseconds.

The two conformations are in equilibrium and transform into one another within one microsecond. The structural similarity of the two conformations explains why they were not previously discovered neither in structural examinations nor in computer simulations. Using time-resolved electron transfer measurements it is now possible to differentiate between and characterize the different states based on their different motilities.

The insights from this study are fundamental to understanding the function of proteins and will help shed light of the mechanisms behind the folding and misfolding of proteins. The scientists now hope to further develop this method in order to apply it to larger proteins important for the regulation of cell functions.


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Contact: Andreas Battenberg
battenberg@zv.tum.de
49-892-891-2890
Technische Universitaet Muenchen
Source:Eurekalert

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