Proton transfer reactions in donor site mutants of ESR, a retinal protein from Exiguobacterium sibiricum
Microbial rhodopsins are integral membrane proteins that contain the retinal chromophore and perform light-dependent ion transport or other functions. The interest in them is largely explained by the perspectives for use in optogenetics in order to regulate the neuronal activity, including for the treatment of various diseases. A team of scientists from the Laboratory of protein engineering and the Group of nanobioengineering of the ICBh RAS has been studying the rhodopsin from Exiguobacterium sibiricum (ESR) for many years. The presence of a lysine residue at position 96 corresponding to the internal proton donor for the Schiff base distinguishes it from bacteriorhodopsin (BR), the most studied retinal protein. In a new study, carried out in collaboration with colleagues from other Russian and foreign institutions, authors have shown that Asp or Glu residues in this position effectively perform the function of a donor in the ESR molecule. However, the kinetics of the photocycle and charge transfer in mutants differ significantly from BR, indicating an alternative mechanism for reprotonation of the Schiff base in ESR. The results are published in the J Photochem Photobiol B.
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Tools created at the Laboratory of Biomolecular Modelling IBCh RAS have been brought together into a computational framework to build a model of SARS-CoV-2 spike transmembrane domain (TMD).
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Methods for inhibition of viral infection induced by spraying plants with preparations of specific double-stranded RNAs (dsRNAs) are currently being actively developed. Researchers from the Laboratory of functional genomics and plant proteomics, the Laboratory of Molecular Diagnostics and the Laboratory of Molecular Bases of Plant Stress Resistance of the Institute of Bioorganic Chemistry RAS studied the contribution of potato plant treatment with dsRNA against potato virus Y (dsRNA-PVY) to two dsRNA-induced plant defense mechanisms: specific RNA interference (RNAi) and non-specific pattern-triggered immunity (PTI).
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