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Articles by Igor Schapiro
Cryo–electron microscopy structures of human cone visual pigments
Editor’s summary Structured Abstract Abstract Supplementary Materials References and Notes Information & Authors Metrics & Citations Check Access References Figures Tables Media Share Editor’s summary Human daytime vision relies on a trio of visual receptors called opsins, which are found in the cone cells in and around the central region of the retina.
Structural insights into light harvesting by antenna-containing rhodopsins in marine Asgard archaea - Nature Microbiology
Abstract Aquatic bacterial rhodopsin proton pumps harvest light energy for photoheterotrophic growth and are known to contain hydroxylated carotenoids that expand the wavelengths of light utilized, but these have not been characterized in marine archaea.
Structural insights into light-gating of potassium-selective channelrhodopsin - Nature Communications
Abstract Structural information on channelrhodopsins’ mechanism of light-gated ion conductance is scarce, limiting its engineering as optogenetic tools. Here, we use single-particle cryo-electron microscopy of peptidisc-incorporated protein samples to determine the structures of the slow-cycling mutant C110A of kalium channelrhodopsin 1 from Hyphochytrium catenoides (HcKCR1) in the dark and upon laser flash excitation.
Structural insights into light-gating of potassium-selective channelrhodopsin
2 days ago I Just Spent The Past 15 Minutes With My Jaw On The Floor After Seeing All These Fascinating Pictures For The First Time And Now I Need You To See Them Truly amazing stuff. Enjoy. 1. These are the contestants for the 1924 Miss America pageant: Looks like they raided the backstage at my high school drama club. 2.
Author Correction: NeoR, a near-infrared absorbing rhodopsin - Nature Communications
Correction to: Nature Communications https://doi.org/10.1038/s41467-020-19375-8, published online 10 November 2020 Since the publication of this work, Enrico Schiewer has changed their name from Enrico Peter. This has now been amended in the HTML and PDF versions of the article.
The Photochemistry and Photophysics of Benzoyl-Carbazole
The Photochemistry and Photophysics of Benzoyl-Carbazole Benzoyl-carbazole and its derivatives are considered a platform for exploring process such as Room Temperature Phosphorescence (RTP) and Thermally Activated Delayed Fluorescence (TADF). They are also reported to exhibit dual emission, but there is a great spectral variability in the relative intensity of the emission bands reported in different studies.
RhoMax: Computational Prediction of Rhodopsin Absorption Maxima Using Geometric Deep Learning
Download Hi-Res ImageDownload to MS-PowerPointCite This:J. Chem. Inf. Model. 2024, XXXX, XXX RETURN TO ARTICLES ASAPMachine Learning and...Machine Learning and Deep LearningNEXT Meitar Sela The Rachel and Selim Benin School of Computer Science and Engineering, The Hebrew University of Jerusalem, Jerusalem 9190401, Israel , Jonathan R.
Transient 2D IR Spectroscopy and Multiscale Simulations Reveal Vibrational Couplings in the Cyanobacteriochrome Slr1393-g3
Transient 2D IR Spectroscopy and Multiscale Simulations Reveal Vibrational Couplings in the Cyanobacteriochrome Slr1393-g3 | Journal of the American Chemical Society
Rhodopsin-bestrophin fusion proteins from unicellular algae form gigantic pentameric ion channels - Nature Structural & Molecular Biology
Abstract Many organisms sense light using rhodopsins, photoreceptive proteins containing a retinal chromophore. Here we report the discovery, structure and biophysical characterization of bestrhodopsins, a microbial rhodopsin subfamily from marine unicellular algae, in which one rhodopsin domain of eight transmembrane helices or, more often, two such domains in tandem, are C-terminally fused to a bestrophin channel.
Ultrafast proton-coupled isomerization in the phototransformation of phytochrome - Nature Chemistry
Abstract The biological function of phytochromes is triggered by an ultrafast photoisomerization of the tetrapyrrole chromophore biliverdin between two rings denoted C and D. The mechanism by which this process induces extended structural changes of the protein is unclear. Here we report ultrafast proton-coupled photoisomerization upon excitation of the parent state (Pfr) of bacteriophytochrome Agp2.
Serial crystallography captures dynamic control of sequential electron and proton transfer events in a flavoenzyme - Nature Chemistry
Abstract Flavin coenzymes are universally found in biological redox reactions. DNA photolyases, with their flavin chromophore (FAD), utilize blue light for DNA repair and photoreduction. The latter process involves two single-electron transfers to FAD with an intermittent protonation step to prime the enzyme active for DNA repair.
Spin-Chemical Effects on Intramolecular Photoinduced Charge Transfer Reactions in Bisphenanthroline Copper(I)-Viologen Dyad Assemblies
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The Effective Conjugation Length Is Responsible for the Red/Green Spectral Tuning in the Cyanobacteriochrome Slr1393g3
Communication The Effective Conjugation Length Is Responsible for the Red/Green Spectral Tuning in the Cyanobacteriochrome Slr1393g3 Dr. Igor Schapiro Corresponding Author E-mail address: igor.schapiro@mail.huji.ac.il http://orcid.org/0000-0001-8536-6869 Fritz Haber Center for Molecular Dynamics Research, Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem, 91904 Israel Search for more papers by this author PDF PDF Share Abstract The origin of the spectral shift from a red‐...
The Effective Conjugation Length is Responsible for the Red/Green Spectral Tuning in the Cyanobacteriochrome Slr1393g3
The origin of the spectral shift from a red‐ to a green‐absorbing form in a cyanobacteriochrome, Slr1393g3, is identified by application of combined quantum mechanics/molecular mechanics simulations. This protein, related to classical phytochromes, carries the open‐chain tetrapyrrole chromophore phycocyanobilin. Our calculations reveal that the effective conjugation length in the chromophore becomes shorter upon conversion from the red to the green form.
A QM/MM study of the initial excited state dynamics of green-absorbing Proteorhodopsin
The primary photochemical reaction of the green-absorbing Proteorhodopsin is studied by means of a hybrid quantum mechanics/molecular mechanics (QM/MM) approach. The simulations are based on a homology model derived from the blue-absorbing Proteorhodopsin crystal structure. The geometry of retinal and the surrounding sidechains in the protein binding pocket were optimized using the QM/MM method.
A QM/MM study of the initial excited state dynamics of green-absorbing proteorhodopsin
The primary photochemical reaction of the green-absorbing proteorhodopsin is studied by means of a hybrid quantum mechanics/molecular mechanics (QM/MM) approach. The simulations are based on a homology model derived from the blue-absorbing proteorhodopsin crystal structure. The geometry of retinal and the surrounding sidechains in the protein binding pocket were optimized using the QM/MM method. Starting from this geometry the isomerization was studied with a relaxed scan along the C C dihedral.
Photoinduced Processes in Nucleic Acids and Proteins: Faraday Discussion
Light induced chemical and physical processes in small organic-/inorganic-/bio-molecules have been a subject of experimental and theoretical research for several decades. Recent advances in high resolution spatio-temporal techniques have offered detailed understanding of excited state processes in small molecules. In sharp contrast, however, information on electronic processes in biomolecules such as isolated proteins and DNA (and their complexes) is still in its infancy.
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