Biophysicists have demonstrated structural changes of a photosynthetic protein in four dimensions

SFB 1078 Biophysik

SFB 1078 Biophysik

A recent Nature Communications publication of several Collaborative Research Centre "Protonation Dynamics in Protein Function" (SFB 1078) projects sheds light into how light energy is converted into a change in protein structure. 

News from Aug 01, 2019

The conversion of light energy into a change in protein structure plays a central role in many areas of life, for example, in vision or photosynthesis. The study under the direction of Prof. Dr. Ilme Schlichting, Director of the Department of Biomolecular Mechanisms, Max-Planck Institute for Medical Research was significantly supported by scientists of the SFB 1078, namely Ramona Schlesinger, Karsten Heyne, and Joachim Heberle and coworkers. Within the framework of this interdisciplinary cooperation, the atomic structure of the ultra-short intermediate states of the light-driven proton pump Bacteriorhodopsin was elucidated at various points in time after photoactivation. It was shown how the molecule retinal, which is the photosensitive center of the protein, changes its structure after absorption of a photon.

The central research goal of the Collaborative Research Centre 1078 is to identify and understand a new key principal in protein science, namely the control and coordination of complex protein function by protonation dynamics.

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