Scientists have used Diamond Light Source and other synchrotrons to reveal the shape of the protein that gives human tissues their elastic properties. This discovery might lead to the development of new synthetic elastic polymers.
An international team of researchers from the UK, Australia, USA and Europe have solved the complex structure of tropoelastin, the main component of elastin. The team used experimental stations at Diamond, the European Synchrotron Radiation Facility (ESRF) in Grenoble, France, and the Advanced Photon Source (APS) in Chicago, USA, to make this breakthrough, the result of more than a decade of international collaboration. Their findings are published in the March issue of science journal PNAS.
Structure of the full-length tropoelastin calculated from X-ray scattering (left), neutron scattering (middle) and a representation of the two combined (right).
Elastin allows tissues in humans and other mammals to stretch, for example when the lungs expand and contract for respiration or when arteries widen and narrow over the course of a billion heart beats.
“The synchrotron technique used was biological solution scattering and we’re currently working on improving I22’s capabilities in this area. We are collaborating with the ESRF and the European Molecular Biology Laboratory (EMBL) Hamburg to develop automation and automated data analysis techniques for solution scattering in biology so we’re hoping to do a lot more of this kind of research on I22 in the future.”
Professor Nick Terrill, Principal Beamline Scientist for the Non-crystalline diffraction beamline (I22), the experimental station used at Diamond
“The full length protein is very flexible and it is not likely to be amenable to crystallographic studies. Small-angle-X-ray-scattering measurements carried out at ESRF beamline ID02 provided crucial initial data,” adds Theyencheri Narayanan, Head of the Structure of Soft Matter Group at the ESRF.
Shape of tropoelastin, the highly-extensible protein that controls human tissue elasticity
Clair Baldock et al
Published online 28 February 2011
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