UEA program at ULTRA integrates international expertise

The Protein Photosensors program on ULTRA is growing its collaborations with a web of international research groups. The ultimate goal of the program is to unravel the microscopic physics of light sensing in living systems.

The principal investigators, Professor Meech of the University of East Anglia and Professor Tonge of Stony Brook University, USA, are working in a collaboration funded by EPSRC and NSF that has been supported at ULTRA since 2009. The program, which investigates the structure and function of light activated proteins, has now grown to encompass collaborations with research groups from around the world. These include:

• biochemists and spectroscopists at Technical University Munich and the University of Hamburg in Germany;
  
  
• the discoverers of the Dronpa photochromic protein in Japan;
  
  
• biophysical researchers at Ecole Polytechnique Laboratoire d'Optique et Biosciences;
  
  
• protein scientists at Institut Laue-Langevin in France;
  
  
• ultrafast optics group at the University of Pécs in Hungary.

All of these have been working with the principle investigators’ research groups to develop further understanding of how these photoactive systems function in nature and could be exploited. The figure is from a recent publication by the collaboration, which was published in Biochemistry (link opens in a new window) and highlighted on the journal’s home page.

The sensitive time resolved vibrational spectroscopy techniques at ULTRA enables the groups to understand the processes occurring at the chromophore, the heart of these complex light sensing proteins. To confirm hypotheses describing these fascinating processes, specialist biochemistry techniques are being applied to generate novel isotopically edited proteins and specific point mutations. These clever modifications to the proteins can cause small but significant changes to the frequencies of vibrations and timescales of reactions. By modifying the chromophore environment in predictable ways it is possible to identify key parts of the mechanism. Replacement of a single amino acid residue within the protein can inhibit or enhance the activity of the proteins, shedding further light on their behaviour.