The members of the rhodopsin family of proteins are involved in many essential light-dependent processes in biology. Specific photoisomerization of the protein-bound retinylidene PSB at a specified wavelength range of light is at the heart of all of these systems. Nonetheless, it has been difficult to reproduce in an engineered system. We have developed rhodopsin mimics, using intracellular lipid binding protein family members as scaffolds, to study fundamental aspects of protein/chromophore interactions. Herein we describe a system that specifically isomerizes the retinylidene protonated Schiff base both thermally and photochemically. This isomerization has been characterized at atomic resolution by quantitatively interconverting the isomers in the crystal both thermally and photochemically. This event is accompanied by a large pKa change of the imine similar to the pKa changes observed in bacteriorhodopsin and visual opsins during isomerization.
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http://dx.doi.org/10.1021/jacs.6b03681 | DOI Listing |
It is now possible to generate large volumes of high-quality images of biomolecules at near-atomic resolution and in near-native states using cryogenic electron microscopy/electron tomography (Cryo-EM/ET). However, the precise annotation of structures like filaments and membranes remains a major barrier towards applying these methods in high-throughput. To address this, we present TARDIS ( ransformer-b sed apid imensionless nstance egmentation), a machine-learning framework for fast and accurate annotation of micrographs and tomograms.
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Institute of Physics and Astronomy, University of Potsdam, 14476 Potsdam-Golm, Germany.
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Physics, Indian Institute of Technology Banaras Hindu University, Indian Institute of Technology (Banaras Hindu University), Department of Physics, Varanasi, Varanasi, Uttar Pradesh, 221005, INDIA.
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View Article and Find Full Text PDFACS Appl Mater Interfaces
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School of Physical Science and Technology, ShanghaiTech University, Shanghai 201210, People's Republic of China.
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