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Despite damage, membrane protein structure can be seen using new X-ray technology, study reveals
Date:12/20/2010

Australian researchers have identified a way to measure the structure of membrane proteins despite being damaged when using X-ray Free-Electron Lasers (XFELs), a discovery that will help fast track the development of targeted drugs using emerging XFELs technology.

About 70% of drugs on the market today depend on the activity of membrane proteins, which are complex molecules that form the membranes of the cells in our body.

A major problem for the design of new pharmaceuticals, often known as the "membrane protein problem", is that they do not form the crystals needed to enable further investigation of the structure to design better drugs.

A major international effort is being mounted to determine the structures of membrane proteins using XFELs - large facilities that create such a bright beam of X-rays it is possible to see the X-ray light bouncing off a single molecule without forming a crystal.

Professor Keith Nugent, Laureate Professor and ARC Federation Fellow and Director of the Australian Research Council Centre of Excellence for Coherent X-ray Science (CXS) at the University of Melbourne said a key problem was that the light from an XFEL was so bright a molecule would start to disintegrate in less than one thousandth of a millionth of a millionth of a second.

In a paper published today in the journal Nature Physics, Professor Nugent and Associate Professor Harry Quiney from the ARC Centre of Excellence for Coherent X-ray Science (CXS) have developed a method by which the damage from the XFEL pulse may be included in the data analysis.

Associate Professor Quiney, also of the School of Physics at the University of Melbourne, said results showed that high-resolution molecular structures may be obtained from X-ray scattering data using a few-femtosecond pulse from an XFEL, even if the interaction resulted in significant electronic damage to the target.

"This result has far-reaching impl
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Contact: Diane Squires
dsquires@unimelb.edu.au
043-275-4232
University of Melbourne
Source:Eurekalert

Page: 1 2

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