Lower and middle part of the zipper rx.

The researchers extended this structure so that they could make independent measurements at the upper, lower and middle part of the zipper. Were applied were applied in turn wound to tiny globules that could be directly manipulated by ‘optical tweezers’ – a tool on the ability of laser beams with a certain type of profile to take nanoscale objects. One end of the protein molecule has been held, and the other was under tension, held but with some freedom of movement, so that folding dynamics could be measured directly, in real time, such as the protein zipped and unpacked rx . States, but also allows measurements with high resolution in time and space. – ‘What I think is the most important improvement is that the new experiments, the observation of thousands of transitions between the folded and unfolded state permit,’Rief said. ‘So we can not only recognize the folded and unfolded states, but also direct the excursions of the large energy barriers between these countries. This is not so far been possible, and it now allows direct insight into the precise energy profile of this obstacle. ‘.

Publication: full distance resolved folding energy landscape of 18th a single protein molecule, by J. Christof M. Gebhart, Thomas Bornschloegl and Matthias Rief, PNAS Early Edition for the week of January 2010.

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