Close This Window

Please download official ILL logos here


For using on the web or on a screenFor printing in high resolutionWhite version, for dark backgrounds

Download PNG

Download AI

Download white PNG

Download JPG


Download white AI

How water molecules dance to activate proteins. 16.03.2015

Back to ILL Homepage
www > Press and news > Press room > Press releases > How water molecules dance to activate proteins. 16.03.2015
English French Deutsch 

Press room

How water molecules dance to activate proteins. 16.03.2015

Water fall. Photo M. Weik

An international team of researchers from the CEA, the CNRS, the Institut Laue-Langevin, the Forschungszentrum Jülich, the University of California Irvine, the Australian Institute of Science and Technology Organisation, the Max Planck Institute Mülheim and the University of Perugia has shed light on the molecular mechanism behind the importance of water for functional protein dynamics. The scientists have discovered that water’s ability to flow on the surface of proteins makes them sufficiently dynamic to be biologically active. The results have just been published in Nature Communication on 16/03/2015.


In order to be biologically active, most soluble proteins require their surface to be covered with water. This so-called hydration water is generally acknowledged to enable a protein to undergo the internal motions that are so fundamental for its capacity to fulfill a specific biological function. Yet, the molecular mechanism behind water’s importance for functional protein dynamics has remained elusive. The team has now been able to observe the movements of water molecules on the surface of proteins. The study highlights how these movements correlate with protein dynamics that is essential to biological activity. Temperature turned out to be an essential parameter; since the motions of water molecules and, therefore, the behaviour of the proteins depend on it.

When "visualising" water movement on the protein surface, the team discovered that the molecules rotate around their own axes at temperatures below  30°C, temperatures at which proteins are inactive. Above  30°C however, whilst continuing to rotate, the water molecules also start to undergo translational diffusion. This is the temperature at which proteins start to be active and the researchers suggest that the capacity of water molecules to "dance" on the surface of proteins enables the dynamics they need to function.

To achieve these results, the scientists combined neutron scattering with molecular dynamics simulations. The neutron scattering technique provides detailed information on the movement and local arrangement of atoms and molecules in matter. The researchers had to first mask the scattering signal of the proteins, whilst preserving the signal from the water molecules on the protein surfaces. To achieve this they produced perdeuterated proteins (proteins in which all the hydrogen atoms are replaced by deuterium atoms) in ILL’s Life Sciences Group.

The study provides a better understanding of the conditions proteins require to be biologically active. An application of the results is the stabilization of protein drugs in the solid state, such as for example insulin that is used for treating diabetes.

For more information please contact Dr. M. Weik, at IBS.


Re.: Nature communications 6,  doi:10.1038/ncomms7490


Notes to editors

About ILL – The Institut Laue-Langevin (ILL) is an international research centre based in Grenoble, France. It has led the world in neutron-scattering science and technology for more than 40 years, since experiments began in 1972. ILL operates one of the most intense neutron sources in the world, feeding beams of neutrons to a suite of 40 high-performance instruments that are constantly upgraded. Each year 1,200 scientists from more than 30 countries worldwide visit ILL (2000 visits), to conduct research into condensed matter physics, (green) chemistry, biology, nuclear physics, and materials science. The UK, along with France and Germany, is an Associate and major funder of the ILL.


About the IBS - The Institut de Biologie Structurale (IBS) is a research centre in structural biology. The IBS performs interdisciplinary research at the interface of biology, physics and chemistry, and combines:   

  • fundamental research
  • technical innovation
  • hosting of scientists
  • training of young researchers
  • a site that facilitates access to European research institutes

The IBS employs approximately 230 people.