Physical Chemistry Chemical Physics, ISSN 1463-9076, 2018, Volume 20, Issue 13, pp. 8450 - 8455
Krokinobacter rhodopsin 2 (KR2), a light-driven Na+ pump, is a dual-functional protein, pumping protons in the absence of Na+ when K+ or larger alkali metal...
TRANSPORT | SOLID-STATE NMR | SPECTROSCOPY | CHROMOPHORE | STRUCTURAL BASIS | PHYSICS, ATOMIC, MOLECULAR & CHEMICAL | GREEN PROTEORHODOPSIN | CHEMISTRY, PHYSICAL | SODIUM-ION PUMP | BACTERIORHODOPSIN | LIGHT-DRIVEN NA+ | WATER-MOLECULE | Rhodopsins, Microbial - genetics | Binding Sites | Proton Pumps - genetics | Rhodopsins, Microbial - chemistry | Schiff Bases - chemistry | Protons | Fourier transforms | Nuclear magnetic resonance--NMR | Pumping | Photolysis | Imines | Alkali metals | Perturbation | Binding sites | Strong interactions (field theory) | Metal ions
TRANSPORT | SOLID-STATE NMR | SPECTROSCOPY | CHROMOPHORE | STRUCTURAL BASIS | PHYSICS, ATOMIC, MOLECULAR & CHEMICAL | GREEN PROTEORHODOPSIN | CHEMISTRY, PHYSICAL | SODIUM-ION PUMP | BACTERIORHODOPSIN | LIGHT-DRIVEN NA+ | WATER-MOLECULE | Rhodopsins, Microbial - genetics | Binding Sites | Proton Pumps - genetics | Rhodopsins, Microbial - chemistry | Schiff Bases - chemistry | Protons | Fourier transforms | Nuclear magnetic resonance--NMR | Pumping | Photolysis | Imines | Alkali metals | Perturbation | Binding sites | Strong interactions (field theory) | Metal ions
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 06/2017, Volume 114, Issue 23, pp. 6028 - 6033
Ci-opsin1 is a visible light-sensitive opsin present in the larval ocellus of an ascidian, Ciona intestinalis. This invertebrate opsin belongs to the...
Molecular evolution | Opsin | G protein-coupled receptors | Ascidian | Counterion | ACTIVATION | VISUAL PIGMENTS | MULTIDISCIPLINARY SCIENCES | opsin | SCHIFF-BASE COUNTERION | GLUTAMIC-ACID | counterion | molecular evolution | PHOTOTRANSDUCTION | ascidian | BOVINE RHODOPSIN | ASCIDIAN CIONA-INTESTINALIS | PROTEIN-COUPLED-RECEPTOR | VERTEBRATE | METARHODOPSIN-II | Biological Sciences
Molecular evolution | Opsin | G protein-coupled receptors | Ascidian | Counterion | ACTIVATION | VISUAL PIGMENTS | MULTIDISCIPLINARY SCIENCES | opsin | SCHIFF-BASE COUNTERION | GLUTAMIC-ACID | counterion | molecular evolution | PHOTOTRANSDUCTION | ascidian | BOVINE RHODOPSIN | ASCIDIAN CIONA-INTESTINALIS | PROTEIN-COUPLED-RECEPTOR | VERTEBRATE | METARHODOPSIN-II | Biological Sciences
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 12/2004, Volume 126, Issue 49, pp. 16018 - 16037
CASPT2//CASSCF photoisomerization path computations have been used to unveil the effects of an acetate counterion on the photochemistry of two retinal...
BOVINE RHODOPSIN | VISUAL PIGMENTS | POTENTIAL-ENERGY SURFACES | SCHIFF-BASE COUNTERION | POINT-CHARGE MODEL | CONICAL INTERSECTION | REACTION-PATH | EXCITED-STATE DYNAMICS | CIS-TRANS PHOTOISOMERIZATION | CHEMISTRY, MULTIDISCIPLINARY | SENSORY RHODOPSIN-II | Chromophores | Structure | Analysis | Isomerization | Chemical models
BOVINE RHODOPSIN | VISUAL PIGMENTS | POTENTIAL-ENERGY SURFACES | SCHIFF-BASE COUNTERION | POINT-CHARGE MODEL | CONICAL INTERSECTION | REACTION-PATH | EXCITED-STATE DYNAMICS | CIS-TRANS PHOTOISOMERIZATION | CHEMISTRY, MULTIDISCIPLINARY | SENSORY RHODOPSIN-II | Chromophores | Structure | Analysis | Isomerization | Chemical models
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 04/2009, Volume 131, Issue 14, pp. 5172 - 5186
Hybrid QM(CASPT2//CASSCF/6−31G*)/MM(Amber) computations have been used to map the photoisomerization path of the retinal chromophore in Rhodopsin and explore...
PERTURBATION-THEORY | MOLECULAR-GENETICS | RHODOPSIN FAMILY | RETINYLIDENE SCHIFF-BASE | RETINAL CHROMOPHORE MODEL | ENERGY-STORAGE | GLUTAMIC-ACID | BINDING POCKET | CHEMISTRY, MULTIDISCIPLINARY | PROTEIN-COUPLED-RECEPTOR | HUMAN COLOR-VISION | Protons | Computational Biology - methods | Ions - chemistry | Retina - metabolism | Models, Molecular | Crystallography, X-Ray | Static Electricity | Isomerism | Thermodynamics | Quantum Theory | Animals | Rhodopsin - genetics | Cattle | Mutation | Binding Sites | Color Vision | Photochemistry | Rhodopsin - chemistry | Optical properties | Analysis | Isomerization | Amino acids | Electrostatic interactions | Chromophores | Chemical properties | Structure | Quantum theory
PERTURBATION-THEORY | MOLECULAR-GENETICS | RHODOPSIN FAMILY | RETINYLIDENE SCHIFF-BASE | RETINAL CHROMOPHORE MODEL | ENERGY-STORAGE | GLUTAMIC-ACID | BINDING POCKET | CHEMISTRY, MULTIDISCIPLINARY | PROTEIN-COUPLED-RECEPTOR | HUMAN COLOR-VISION | Protons | Computational Biology - methods | Ions - chemistry | Retina - metabolism | Models, Molecular | Crystallography, X-Ray | Static Electricity | Isomerism | Thermodynamics | Quantum Theory | Animals | Rhodopsin - genetics | Cattle | Mutation | Binding Sites | Color Vision | Photochemistry | Rhodopsin - chemistry | Optical properties | Analysis | Isomerization | Amino acids | Electrostatic interactions | Chromophores | Chemical properties | Structure | Quantum theory
Journal Article
Biochemistry, ISSN 0006-2960, 07/2012, Volume 51, Issue 29, pp. 5748 - 5762
One of the distinctive features of eubacterial retinal-based proton pumps, proteorhodopsins, xanthorhodopsin, and others, is hydrogen bonding of the key...
PHOTOCHEMICAL CYCLE | TRANSITION | TRANSLOCATION | XANTHORHODOPSIN | PROTEORHODOPSIN | CHROMOPHORE | PHOTOISOMERIZATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | BACTERIORHODOPSIN PHOTOCYCLE | RELEASE | Protons | Bacillales - chemistry | Bacterial Proteins - chemistry | Histidine - metabolism | Photochemical Processes | Aspartic Acid - genetics | Rhodopsins, Microbial - metabolism | Cloning, Molecular | Bacillales - genetics | Rhodopsins, Microbial - genetics | Bacterial Proteins - genetics | Histidine - genetics | Models, Molecular | Spectrometry, Fluorescence | Escherichia coli - genetics | Schiff Bases - chemistry | Aspartic Acid - metabolism | Bacillales - metabolism | Bacterial Proteins - metabolism | Schiff Bases - metabolism | Aspartic Acid - chemistry | Kinetics | Mutation | Histidine - chemistry | Rhodopsins, Microbial - chemistry | Schiff bases | Histidine | Analysis | Emission | Aspartate | Absorption of light | Chemical properties | Hydrogen bonding | Protein-protein interactions | Electrons
PHOTOCHEMICAL CYCLE | TRANSITION | TRANSLOCATION | XANTHORHODOPSIN | PROTEORHODOPSIN | CHROMOPHORE | PHOTOISOMERIZATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | BACTERIORHODOPSIN PHOTOCYCLE | RELEASE | Protons | Bacillales - chemistry | Bacterial Proteins - chemistry | Histidine - metabolism | Photochemical Processes | Aspartic Acid - genetics | Rhodopsins, Microbial - metabolism | Cloning, Molecular | Bacillales - genetics | Rhodopsins, Microbial - genetics | Bacterial Proteins - genetics | Histidine - genetics | Models, Molecular | Spectrometry, Fluorescence | Escherichia coli - genetics | Schiff Bases - chemistry | Aspartic Acid - metabolism | Bacillales - metabolism | Bacterial Proteins - metabolism | Schiff Bases - metabolism | Aspartic Acid - chemistry | Kinetics | Mutation | Histidine - chemistry | Rhodopsins, Microbial - chemistry | Schiff bases | Histidine | Analysis | Emission | Aspartate | Absorption of light | Chemical properties | Hydrogen bonding | Protein-protein interactions | Electrons
Journal Article
Inorganic Chemistry, ISSN 0020-1669, 09/2016, Volume 55, Issue 17, pp. 8260 - 8262
Chiral and racemic 68-membered [4 + 4] tetranuclear and 34-membered [2 + 2] dinuclear Schiff-base macrocyclic zinc(II) complexes 1–10 can be selectively...
RECOGNITION | PSEUDOPEPTIDIC MACROCYCLES | EXPANSION | ION | DYNAMIC COMBINATORIAL CHEMISTRY | TEMPLATE | CHEMISTRY, INORGANIC & NUCLEAR | Schiff bases | Zinc compounds | Chemical properties | Chirality | Analysis
RECOGNITION | PSEUDOPEPTIDIC MACROCYCLES | EXPANSION | ION | DYNAMIC COMBINATORIAL CHEMISTRY | TEMPLATE | CHEMISTRY, INORGANIC & NUCLEAR | Schiff bases | Zinc compounds | Chemical properties | Chirality | Analysis
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2003, Volume 100, Issue 16, pp. 9262 - 9267
The biological function of Glu-181 in the photoactivation process of rhodopsin is explored through spectroscopic studies of site-specific mutants. Preresonance...
Protons | Biological Sciences | Receptors | Wavelengths | Retinal pigments | Disulfides | Pigments | Biochemistry | Chromophores | Absorption spectra | Electrostatics | CYTOPLASMIC SURFACE | CYSTEINE RESIDUE-110 | CHROMOPHORE BINDING-SITE | BOVINE RHODOPSIN | VISUAL PIGMENTS | MULTIDISCIPLINARY SCIENCES | SCHIFF-BASE COUNTERION | DISULFIDE BOND | GLUTAMIC-ACID | RETINITIS-PIGMENTOSA | METARHODOPSIN-II | GTP-Binding Proteins - physiology | Retina - metabolism | Temperature | Mutagenesis, Site-Directed | GTP-Binding Proteins - chemistry | Models, Chemical | Models, Molecular | Ions | Animals | Rhodopsin - analogs & derivatives | Ultraviolet Rays | Cattle | Light | Protein Binding | Spectrum Analysis, Raman | Rhodopsin - physiology | Glutamic Acid - chemistry | Hydrogen-Ion Concentration | Rhodopsin - chemistry | Molecules | Biology | Research
Protons | Biological Sciences | Receptors | Wavelengths | Retinal pigments | Disulfides | Pigments | Biochemistry | Chromophores | Absorption spectra | Electrostatics | CYTOPLASMIC SURFACE | CYSTEINE RESIDUE-110 | CHROMOPHORE BINDING-SITE | BOVINE RHODOPSIN | VISUAL PIGMENTS | MULTIDISCIPLINARY SCIENCES | SCHIFF-BASE COUNTERION | DISULFIDE BOND | GLUTAMIC-ACID | RETINITIS-PIGMENTOSA | METARHODOPSIN-II | GTP-Binding Proteins - physiology | Retina - metabolism | Temperature | Mutagenesis, Site-Directed | GTP-Binding Proteins - chemistry | Models, Chemical | Models, Molecular | Ions | Animals | Rhodopsin - analogs & derivatives | Ultraviolet Rays | Cattle | Light | Protein Binding | Spectrum Analysis, Raman | Rhodopsin - physiology | Glutamic Acid - chemistry | Hydrogen-Ion Concentration | Rhodopsin - chemistry | Molecules | Biology | Research
Journal Article
Nature Structural & Molecular Biology, ISSN 1545-9993, 03/2004, Volume 11, Issue 3, pp. 284 - 289
The counterion, a negatively charged amino acid residue that stabilizes a positive charge on the retinylidene chromophore, is essential for rhodopsin to...
RETINOCHROME | NEUROTRANSMITTER RECEPTORS | BIOCHEMISTRY & MOLECULAR BIOLOGY | LIGHT | OPSIN | INVERTEBRATE VISUAL PIGMENTS | CELL BIOLOGY | COLOR-VISION | BIOPHYSICS | BOVINE RHODOPSIN | SCHIFF-BASE | PROTEIN-COUPLED-RECEPTOR | VERTEBRATE | Glutamic Acid | Anions | Animals | Mutagenesis, Site-Directed | Rhodopsin - genetics | Retinoids - chemistry | Phylogeny | Amino Acids, Acidic - chemistry | Evolution, Molecular | GTP-Binding Proteins - metabolism | Rhodopsin - chemistry | Physiological aspects | Rhodopsin | Research | G proteins | Glutamate | Structure
RETINOCHROME | NEUROTRANSMITTER RECEPTORS | BIOCHEMISTRY & MOLECULAR BIOLOGY | LIGHT | OPSIN | INVERTEBRATE VISUAL PIGMENTS | CELL BIOLOGY | COLOR-VISION | BIOPHYSICS | BOVINE RHODOPSIN | SCHIFF-BASE | PROTEIN-COUPLED-RECEPTOR | VERTEBRATE | Glutamic Acid | Anions | Animals | Mutagenesis, Site-Directed | Rhodopsin - genetics | Retinoids - chemistry | Phylogeny | Amino Acids, Acidic - chemistry | Evolution, Molecular | GTP-Binding Proteins - metabolism | Rhodopsin - chemistry | Physiological aspects | Rhodopsin | Research | G proteins | Glutamate | Structure
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 12/2006, Volume 128, Issue 51, pp. 16502 - 16503
Photoisomerization of the retinylidene chromophore of rhodopsin is the starting point in the vision cascade. A counterion switch mechanism that stabilizes the...
ACTIVATION | PERSPECTIVE | RHODOPSIN | DYNAMICS | METARHODOPSIN-I | NMR STRUCTURE | STATE | CRYSTALLOGRAPHY | PHOTOACTIVATION | CHEMISTRY, MULTIDISCIPLINARY | PROTEIN-COUPLED-RECEPTOR | Thermodynamics | Magnetic Resonance Spectroscopy - methods | Models, Biological | Vision, Ocular | Computer Simulation | Schiff Bases - chemistry | Sensitivity and Specificity | Molecular Structure | Rhodopsin - chemical synthesis | Rhodopsin - chemistry | Molecular dynamics | Schiff bases | Rhodopsin | Chemical properties | Analysis
ACTIVATION | PERSPECTIVE | RHODOPSIN | DYNAMICS | METARHODOPSIN-I | NMR STRUCTURE | STATE | CRYSTALLOGRAPHY | PHOTOACTIVATION | CHEMISTRY, MULTIDISCIPLINARY | PROTEIN-COUPLED-RECEPTOR | Thermodynamics | Magnetic Resonance Spectroscopy - methods | Models, Biological | Vision, Ocular | Computer Simulation | Schiff Bases - chemistry | Sensitivity and Specificity | Molecular Structure | Rhodopsin - chemical synthesis | Rhodopsin - chemistry | Molecular dynamics | Schiff bases | Rhodopsin | Chemical properties | Analysis
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 09/2010, Volume 132, Issue 38, pp. 13104 - 13107
The stereochemistry-determining step of the self-assembled chiral Brønsted acid-catalyzed aziridination reactions of MEDAM imines and three representative...
ACID | MECHANISM | IMINES | ACYLDIAZOMETHANES | CONDENSATION | ALDEHYDES | CHEMISTRY, MULTIDISCIPLINARY | CATALYTIC ASYMMETRIC AZIRIDINATION | DIAZOACETAMIDES | Boron Compounds - chemistry | Models, Molecular | Catalysis | Hydrogen Bonding | Aziridines - chemistry | Stereoisomerism | Diazo compounds | Schiff bases | Analysis | Chirality | Chemical properties | Structure | Hydrogen bonding
ACID | MECHANISM | IMINES | ACYLDIAZOMETHANES | CONDENSATION | ALDEHYDES | CHEMISTRY, MULTIDISCIPLINARY | CATALYTIC ASYMMETRIC AZIRIDINATION | DIAZOACETAMIDES | Boron Compounds - chemistry | Models, Molecular | Catalysis | Hydrogen Bonding | Aziridines - chemistry | Stereoisomerism | Diazo compounds | Schiff bases | Analysis | Chirality | Chemical properties | Structure | Hydrogen bonding
Journal Article
Inorganica Chimica Acta, ISSN 0020-1693, 05/2019, Volume 490, pp. 51 - 56
The first Cu-Ln Schiff base complexes containing [Ln( -diketone) ] blocks have been obtained and the Cu-Tb complex exhibits slow magnetic relaxation behavior....
Schiff base | Slow magnetic relaxation | Heterometallic complexes | Ln(hfac)4 | Protons | Magnetic induction | Imines | Magnetic relaxation | Gadolinium | Ferromagnetism | Structural analysis | Magnetic measurement
Schiff base | Slow magnetic relaxation | Heterometallic complexes | Ln(hfac)4 | Protons | Magnetic induction | Imines | Magnetic relaxation | Gadolinium | Ferromagnetism | Structural analysis | Magnetic measurement
Journal Article
INORGANICA CHIMICA ACTA, ISSN 0020-1693, 05/2019, Volume 490, pp. 51 - 56
Two novel heterometallic Cu-Ln Schiff base complexes {[Ln(hfac)(2)Cu(L)(H2O)][Ln(hfac)(4)][CuL]}(Ln(III) = Gd 1, Tb 2, hfac = hexafluoroacetylacetone; H2L =...
GD-III | SINGLE-MOLECULE-MAGNET | TB-III | Ln(hfac)(-) | BEHAVIOR | ANISOTROPY | CHEMISTRY, INORGANIC & NUCLEAR | Schiff base | STRUCTURAL DETERMINATION | Slow magnetic relaxation | CO-II | LANTHANIDE | TRINUCLEAR | Heterometallic complexes
GD-III | SINGLE-MOLECULE-MAGNET | TB-III | Ln(hfac)(-) | BEHAVIOR | ANISOTROPY | CHEMISTRY, INORGANIC & NUCLEAR | Schiff base | STRUCTURAL DETERMINATION | Slow magnetic relaxation | CO-II | LANTHANIDE | TRINUCLEAR | Heterometallic complexes
Journal Article
Inorganica Chimica Acta, ISSN 0020-1693, 08/2013, Volume 405, pp. 182 - 187
Three new salen type Ce(IV) complexes, have been synthesized and structurally determined. Their electrochemical properties are investigated and discussed....
Electrochemistry | Synthesis | Salen type | Structure | Mononuclear cerium complexes | SINGLE-MOLECULE MAGNET | 3D-4F COMPLEXES | CRYSTAL-STRUCTURE | COORDINATION | CHEMISTRY, INORGANIC & NUCLEAR | NEAR-INFRARED NIR | SENSITIZED LUMINESCENCE | LN(SALEN) | SLOW MAGNETIC-RELAXATION | SCHIFF-BASE COMPLEXES | Cerium | Electrochemical reactions
Electrochemistry | Synthesis | Salen type | Structure | Mononuclear cerium complexes | SINGLE-MOLECULE MAGNET | 3D-4F COMPLEXES | CRYSTAL-STRUCTURE | COORDINATION | CHEMISTRY, INORGANIC & NUCLEAR | NEAR-INFRARED NIR | SENSITIZED LUMINESCENCE | LN(SALEN) | SLOW MAGNETIC-RELAXATION | SCHIFF-BASE COMPLEXES | Cerium | Electrochemical reactions
Journal Article
Theoretical Chemistry Accounts, ISSN 1432-881X, 09/2004, Volume 112, Issue 4, pp. 335 - 341
A special hybrid quantum mechanics/molecular mechanics forcefield is defined, parameterized and validated for studying the photoisomerization path of the...
Chemistry | Rhodopsin | Quantum mechanics/Molecular mechanics | Parameterization | Photoisomerization | Retinal | rhodopsin | retinal | quantum mechanics | molecular mechanics | RESP | CHARGES | photoisomerization | parameterization | CHEMISTRY, PHYSICAL | PROTONATED SCHIFF-BASE | MODEL | SIMULATIONS
Chemistry | Rhodopsin | Quantum mechanics/Molecular mechanics | Parameterization | Photoisomerization | Retinal | rhodopsin | retinal | quantum mechanics | molecular mechanics | RESP | CHARGES | photoisomerization | parameterization | CHEMISTRY, PHYSICAL | PROTONATED SCHIFF-BASE | MODEL | SIMULATIONS
Journal Article
Biochemistry, ISSN 0006-2960, 11/2010, Volume 49, Issue 47, pp. 10089 - 10097
Visual pigments consist of a protein moiety opsin and an 11-cis-retinal chromophore that is covalently bound to the opsin via a Schiff base linkage. They have...
ACTIVATION | CONGENITAL NIGHT BLINDNESS | BOVINE RHODOPSIN | CHROMOPHORE | VISUAL PIGMENTS | PHOTOISOMERIZATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | SCHIFF-BASE COUNTERION | LUMI-RHODOPSIN | META-RHODOPSIN | DROSOPHILA RHODOPSIN | Amino Acid Sequence | Animals | Rhodopsin - genetics | Cattle | Drug Stability | Schiff Bases - chemistry | Models, Molecular | Mutation | Rhodopsin - radiation effects | Spectrophotometry, Ultraviolet | Amino Acid Substitution | Rhodopsin - chemistry | Schiff bases | Rhodopsin | Amines | Isomerization | Analysis | Chemical properties | Structure
ACTIVATION | CONGENITAL NIGHT BLINDNESS | BOVINE RHODOPSIN | CHROMOPHORE | VISUAL PIGMENTS | PHOTOISOMERIZATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | SCHIFF-BASE COUNTERION | LUMI-RHODOPSIN | META-RHODOPSIN | DROSOPHILA RHODOPSIN | Amino Acid Sequence | Animals | Rhodopsin - genetics | Cattle | Drug Stability | Schiff Bases - chemistry | Models, Molecular | Mutation | Rhodopsin - radiation effects | Spectrophotometry, Ultraviolet | Amino Acid Substitution | Rhodopsin - chemistry | Schiff bases | Rhodopsin | Amines | Isomerization | Analysis | Chemical properties | Structure
Journal Article
Inorganica Chimica Acta, ISSN 0020-1693, 05/2019, Volume 490, p. 51
Two novel heterometallic Cu-Ln Schiff base complexes {[Ln(hfac).sub.2Cu(L)(H.sub.2O)][Ln(hfac).sub.4][CuL]}(Ln.sup.III = Gd 1, Tb 2, hfac =...
Schiff bases | Analysis | Ferromagnetism
Schiff bases | Analysis | Ferromagnetism
Journal Article
Photochemical and Photobiological Sciences, ISSN 1474-905X, 11/2010, Volume 9, Issue 11, pp. 1426 - 1434
In rhodopsins, visible-light absorption is achieved by the protonation of the chromophore Schiff base. The Schiff base proton is stabilized by the negative...
SQUID RHODOPSIN | PHOTOISOMERIZATION EFFICIENCY | CONGENITAL NIGHT BLINDNESS | BIOCHEMISTRY & MOLECULAR BIOLOGY | GLUTAMIC-ACID 181 | CHEMISTRY, PHYSICAL | INVERTEBRATE VISUAL PIGMENTS | BIOPHYSICS | CHROMOPHORES IN-VACUO | BOVINE RHODOPSIN | RETINAL CHROMOPHORE | HYDROGEN-BOND NETWORK | PROTEIN-COUPLED-RECEPTOR | Protons | Ions - chemistry | Animals | Opsins - chemistry | Cattle | Schiff Bases - chemistry | Models, Molecular | Isomerism | Photochemistry | Rhodopsin - chemistry
SQUID RHODOPSIN | PHOTOISOMERIZATION EFFICIENCY | CONGENITAL NIGHT BLINDNESS | BIOCHEMISTRY & MOLECULAR BIOLOGY | GLUTAMIC-ACID 181 | CHEMISTRY, PHYSICAL | INVERTEBRATE VISUAL PIGMENTS | BIOPHYSICS | CHROMOPHORES IN-VACUO | BOVINE RHODOPSIN | RETINAL CHROMOPHORE | HYDROGEN-BOND NETWORK | PROTEIN-COUPLED-RECEPTOR | Protons | Ions - chemistry | Animals | Opsins - chemistry | Cattle | Schiff Bases - chemistry | Models, Molecular | Isomerism | Photochemistry | Rhodopsin - chemistry
Journal Article
RSC Advances, ISSN 2046-2069, 2015, Volume 5, Issue 6, pp. 4716 - 4726
Quinoline quaternary ammonium salts 1-benzylquinoline bromide (1) and 1-benzylquinoline chloride (2) have been synthesized and then developed as corrosion...
GEMINI SURFACTANT | ALUMINUM-ALLOY | COLD-ROLLED STEEL | M HYDROCHLORIC-ACID | METAL DISSOLUTION | SULFURIC-ACID | SCHIFF-BASE | IODIDE-IONS | ADSORPTION PROCESSES | CHEMISTRY, MULTIDISCIPLINARY | 0.5 M H2SO4
GEMINI SURFACTANT | ALUMINUM-ALLOY | COLD-ROLLED STEEL | M HYDROCHLORIC-ACID | METAL DISSOLUTION | SULFURIC-ACID | SCHIFF-BASE | IODIDE-IONS | ADSORPTION PROCESSES | CHEMISTRY, MULTIDISCIPLINARY | 0.5 M H2SO4
Journal Article
RSC Advances, 12/2014, Volume 5, Issue 6, pp. 4716 - 4726
Quinoline quaternary ammonium salts 1-benzylquinoline bromide (1) and 1-benzylquinoline chloride (2) have been synthesized and then developed as corrosion...
Thermodynamics | Corrosion inhibitors | Corrosion | Chlorides | Corrosion effects | Carbon steels | Inhibition | Protective coatings | Gravimeters
Thermodynamics | Corrosion inhibitors | Corrosion | Chlorides | Corrosion effects | Carbon steels | Inhibition | Protective coatings | Gravimeters
Journal Article
Scientific Reports, ISSN 2045-2322, 11/2016, Volume 6, Issue 1, p. 36208
The diagnoses of retinitis pigmentosa (RP) and stationary night blindness (CSNB) are two distinct clinical entities belonging to a group of clinically and...
Amino Acid Sequence | Humans | Middle Aged | Retinitis Pigmentosa - genetics | Male | Mutation, Missense | Night Blindness - diagnostic imaging | Retinitis Pigmentosa - diagnostic imaging | Sequence Analysis, DNA | Case-Control Studies | Phenotype | Rhodopsin - genetics | DNA Mutational Analysis | Pedigree | Aged, 80 and over | Adult | Female | Heterozygote | Schiff Bases | Night Blindness - genetics | Amino Acid Substitution | Rhodopsin - chemistry | Rhodopsin | Retinitis pigmentosa | Blindness | Retina | Retinitis | Mutation | Nyctalopia | Stationary night blindness
Amino Acid Sequence | Humans | Middle Aged | Retinitis Pigmentosa - genetics | Male | Mutation, Missense | Night Blindness - diagnostic imaging | Retinitis Pigmentosa - diagnostic imaging | Sequence Analysis, DNA | Case-Control Studies | Phenotype | Rhodopsin - genetics | DNA Mutational Analysis | Pedigree | Aged, 80 and over | Adult | Female | Heterozygote | Schiff Bases | Night Blindness - genetics | Amino Acid Substitution | Rhodopsin - chemistry | Rhodopsin | Retinitis pigmentosa | Blindness | Retina | Retinitis | Mutation | Nyctalopia | Stationary night blindness
Journal Article
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