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Opsin
Animal opsins are G-protein-coupled receptors and a group of proteins made light-sensitive via a chromophore, typically retinal. When bound to retinal, opsins become retinylidene proteins, but are usually still called opsins regardless. Most prominently, they are found in photoreceptor cells of the retina. Five classical groups of opsins are involved in Visual perception, vision, mediating the conversion of a photon of light into an electrochemical signal, the first step in the Visual phototransduction, visual transduction cascade. Another opsin found in the mammalian retina, melanopsin, is involved in circadian rhythms and Pupillary light reflex, pupillary reflex but not in vision. Humans have in total nine opsins. Beside vision and light perception, opsins may also sense temperature, sound, or chemicals. Structure and function Animal opsins detect light and are the molecules that allow us to see. Opsins are G-protein-coupled receptors (GPCRs), which are chemoreceptors and hav ...
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Rhodopsin 3D
Rhodopsin, also known as visual purple, is a protein encoded by the ''RHO'' gene and a G-protein-coupled receptor (GPCR). It is a light-sensitive receptor protein that triggers visual phototransduction in rod cells. Rhodopsin mediates dim light vision and thus is extremely sensitive to light. When rhodopsin is exposed to light, it immediately photobleaches. In humans, it is fully regenerated in about 30 minutes, after which the rods are more sensitive. Defects in the rhodopsin gene cause eye diseases such as retinitis pigmentosa and congenital stationary night blindness. History Rhodopsin was discovered by Franz Christian Boll in 1876. The name rhodopsin derives from Ancient Greek () for "rose", due to its pinkish color, and () for "sight". It was coined in 1878 by the German physiologist Wilhelm Friedrich Kühne (1837–1900). When George Wald discovered that rhodopsin is a holoprotein, consisting of retinal and an apoprotein, he called it opsin, which today ...
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Melanopsin
Melanopsin is a type of photopigment belonging to a larger family of light-sensitive retinylidene protein, retinal proteins called opsins and encoded by the gene ''Opn4''. In the mammalian retina, there are two additional categories of opsins, both involved in the formation of visual images: rhodopsin and photopsin (types I, II, and III) in the Rod cell, rod and Cone cell, cone photoreceptor cells, respectively. In humans, melanopsin is found in intrinsically photosensitive retinal ganglion cells (ipRGCs). It is also found in the iris of mice and primates. Melanopsin is also found in rats, amphioxus, and other chordates. ipRGCs are photoreceptor cells which are particularly sensitive to the absorption of short-wavelength (blue) visible light and communicate information directly to the area of the brain called the suprachiasmatic nucleus (SCN), also known as the central "body clock", in mammals. Melanopsin plays an important non-image-forming role in the Entrainment (chronobiology ...
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Visual Phototransduction
Visual phototransduction is the sensory transduction process of the visual system by which light is detected by photoreceptor cells ( rods and cones) in the vertebrate retina. A photon is absorbed by a retinal chromophore (each bound to an opsin), which initiates a signal cascade through several intermediate cells, then through the retinal ganglion cells (RGCs) comprising the optic nerve. Overview Light enters the eye, passes through the optical media, then the inner neural layers of the retina before finally reaching the photoreceptor cells in the outer layer of the retina. The light may be absorbed by a chromophore bound to an opsin, which photoisomerizes the chromophore, initiating both the visual cycle, which "resets" the chromophore, and the phototransduction cascade, which transmits the visual signal to the brain. The cascade begins with graded polarisation (an analog signal) of the excited photoreceptor cell, as its membrane potential increases from a resting po ...
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Phototransduction Cascade
Visual phototransduction is the sensory transduction process of the visual system by which light is detected by photoreceptor cells ( rods and cones) in the vertebrate retina. A photon is absorbed by a retinal chromophore (each bound to an opsin), which initiates a signal cascade through several intermediate cells, then through the retinal ganglion cells (RGCs) comprising the optic nerve. Overview Light enters the eye, passes through the optical media, then the inner neural layers of the retina before finally reaching the photoreceptor cells in the outer layer of the retina. The light may be absorbed by a chromophore bound to an opsin, which photoisomerizes the chromophore, initiating both the visual cycle, which "resets" the chromophore, and the phototransduction cascade, which transmits the visual signal to the brain. The cascade begins with graded polarisation (an analog signal) of the excited photoreceptor cell, as its membrane potential increases from a resting potential of - ...
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Retinylidene Protein
Retinylidene proteins, or rhodopsins in a broad sense, are proteins that use retinal as a chromophore for light reception. They are the molecular basis for a variety of light-sensing systems from phototaxis in flagellates to eyesight in animals. Retinylidene proteins include all forms of opsin and rhodopsin (in the broad sense). While rhodopsin in the narrow sense refers to a dim-light visual pigment found in vertebrates, usually on rod cells, ''rhodopsin'' in the broad sense (as used here) refers to any molecule consisting of an opsin and a retinal chromophore in the ground state. When activated by light, the chromophore is isomerized, at which point the molecule as a whole is no longer rhodopsin, but a related molecule such as metarhodopsin. However, it remains a retinylidene protein. The chromophore then separates from the opsin, at which point the bare opsin is a retinylidene protein. Thus, the molecule remains a retinylidene protein throughout the phototransduction cycle. S ...
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Retinal
Retinal (also known as retinaldehyde) is a polyene chromophore. Retinal, bound to proteins called opsins, is the chemical basis of visual phototransduction, the light-detection stage of visual perception (vision). Some microorganisms use retinal to convert light into metabolic energy. One study suggests that approximately three billion years ago, most living organisms on Earth used retinal, rather than chlorophyll, to convert sunlight into energy. Because retinal absorbs mostly green light and transmits purple light, this gave rise to the Purple Earth hypothesis. Retinal itself is considered to be a form of vitamin A when eaten by an animal. There are many forms of vitamin A, all of which are converted to retinal, which cannot be made without them. The number of different molecules that can be converted to retinal varies from species to species. Retinal was originally called retinene, and was renamed after it was discovered to be vitamin A aldehyde. Vertebrate animals inge ...
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G-protein-coupled Receptor
G protein-coupled receptors (GPCRs), also known as seven-(pass)-transmembrane domain receptors, 7TM receptors, heptahelical receptors, serpentine receptors, and G protein-linked receptors (GPLR), form a large protein family, group of evolutionarily related proteins that are cell surface receptors that detect molecules outside the cell (biology), cell and activate cellular responses. They are coupled with G proteins. They pass through the cell membrane seven times in the form of six loops (three extracellular loops interacting with ligand molecules, three intracellular loops interacting with G proteins, an N-terminus, N-terminal extracellular region and a C-terminal intracellular region) of amino acid residues, which is why they are sometimes referred to as seven-transmembrane receptors. Text was copied from this source, which is available under Attribution 2.5 Generic (CC BY 2.5) licence/ref> Ligands can bind either to the extracellular N-terminus and loops (e.g. glutama ...
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Vitamin A
Vitamin A is a fat-soluble vitamin that is an essential nutrient. The term "vitamin A" encompasses a group of chemically related organic compounds that includes retinol, retinyl esters, and several provitamin (precursor) carotenoids, most notably Β-Carotene, β-carotene (''beta''-carotene). Vitamin A has multiple functions: growth during embryo development, maintaining the immune system, and healthy vision. For aiding vision specifically, it combines with the protein opsin to form rhodopsin, the light-absorbing molecule necessary for both low-light (scotopic vision) and color vision. Vitamin A occurs as two principal forms in foods: A) retinoids, found in Animal source foods, animal-sourced foods, either as retinol or bound to a fatty acid to become a retinyl ester, and B) the carotenoids Α-Carotene, α-carotene (''alpha''-carotene), β-carotene, Γ-Carotene, γ-carotene (''gamma''-carotene), and the xanthophyll beta-cryptoxanthin (all of which contain β-ionone rings) that ...
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Photoreceptor Cell
A photoreceptor cell is a specialized type of neuroepithelial cell found in the retina that is capable of visual phototransduction. The great biological importance of photoreceptors is that they convert light (visible electromagnetic radiation) into signals that can stimulate biological processes. To be more specific, photoreceptor proteins in the cell absorb photons, triggering a change in the cell's membrane potential. There are currently three known types of photoreceptor cells in mammalian eyes: rod cell, rods, cone cell, cones, and intrinsically photosensitive retinal ganglion cells. The two classic photoreceptor cells are rods and cones, each contributing information used by the visual system to form an image of the environment, Visual perception, sight. Rods primarily mediate scotopic vision (dim conditions) whereas cones primarily mediate photopic vision (bright conditions), but the processes in each that supports phototransduction is similar. The intrinsically photosen ...
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Photoreceptor Protein
Photoreceptor proteins are light-sensitive proteins involved in the sensing and response to light in a variety of organisms. Some examples are rhodopsin in the photoreceptor cells of the vertebrate retina, phytochrome in plants, and bacteriorhodopsin and bacteriophytochromes in some bacteria. They mediate light responses as varied as visual perception, phototropism and phototaxis, as well as responses to light-dark cycles such as circadian rhythm and other photoperiodisms including control of flowering times in plants and mating seasons in animals. Structure Photoreceptor proteins typically consist of a protein attached to a non-protein chromophore (sometimes referred as photopigment, even so photopigment may also refer to the photoreceptor as a whole). The chromophore reacts to light via photoisomerization or photoreduction, thus initiating a change of the receptor protein which triggers a signal transduction cascade. Chromophores found in photoreceptors include retinal ( ...
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Retina
The retina (; or retinas) is the innermost, photosensitivity, light-sensitive layer of tissue (biology), tissue of the eye of most vertebrates and some Mollusca, molluscs. The optics of the eye create a focus (optics), focused two-dimensional image of the visual world on the retina, which then processes that image within the retina and sends nerve impulses along the optic nerve to the visual cortex to create visual perception. The retina serves a function which is in many ways analogous to that of the photographic film, film or image sensor in a camera. The neural retina consists of several layers of neurons interconnected by Chemical synapse, synapses and is supported by an outer layer of pigmented epithelial cells. The primary light-sensing cells in the retina are the photoreceptor cells, which are of two types: rod cell, rods and cone cell, cones. Rods function mainly in dim light and provide monochromatic vision. Cones function in well-lit conditions and are responsible fo ...
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Lysine
Lysine (symbol Lys or K) is an α-amino acid that is a precursor to many proteins. Lysine contains an α-amino group (which is in the protonated form when the lysine is dissolved in water at physiological pH), an α-carboxylic acid group (which is in the deprotonated form when the lysine is dissolved in water at physiological pH), and a side chain (which is partially protonated when the lysine is dissolved in water at physiological pH), and so it is classified as a basic, charged (in water at physiological pH), aliphatic amino acid. It is encoded by the codons AAA and AAG. Like almost all other amino acids, the α-carbon is chiral and lysine may refer to either enantiomer or a racemic mixture of both. For the purpose of this article, lysine will refer to the biologically active enantiomer L-lysine, where the α-carbon is in the ''S'' configuration. The human body cannot synthesize lysine. It is essential in humans and must therefore be obtained from the diet. In orga ...
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