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Topic: Iodopsin

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	iodopsin - Search Results - MSN Encarta
		Iodopsin definition, words related to iodopsin, proper usage and pronunciation of the word iodopsin...
		Humans have inherited a colour visual system that is dependant upon three forms of iodopsin, or colour pigments, each responding to light of a different wavelength region.
		The cones secrete the pigment iodopsin and are most effective in bright light; they alone provide color vision.
	ca.encarta.msn.com /iodopsin.html (125 words)

	[No title]
		The difference in the photoresponses between color vision and scotopic vision was thought to be due to the differences in structure and photobleaching process between iodopsin and rhodopsin, but the iodopsin was less investigated because the amount of iodopsin in the retina was small and the purification was difficult.
		The chromophore structures of iodopsin and its intermediates were studied by the combination of low-temperature spectroscopy and HPLC analysis [36].
		Raman spectroscopy of iodopsin revealed that the red-shifted absorption spectrum of iodopsin is due to the weaker interaction between Schiff base and the counterion [21].
	mswebs.aist-nara.ac.jp /LABs/kataoka/members/imamoto/english/research/research.html (977 words)

	Iodopsin, a red-sensitive cone visual pigment in the chicken retina.
		Iodopsin, the chicken red-sensitive cone visual pigment, is located at outer segments of both the red single cones and the double cones, while the other single cones and the rod contain their own visual pigments with different absorption spectra.
		That the sensitivity of cones is lower than rods cannot be explained by the relative photosensitivity of iodopsin to rhodopsin, but may be understood to some extent by the short lifetime of an enzymatically active intermediate (corresponding to metarhodopsin II) produced in the photobleaching process of iodopsin.
		The rapid formation and decay of the meta II-intermediate of iodopsin compared with metarhodopsin II are not contradictory to the rapid generation and recovery of cone receptor potential compared with rod receptor potential.
	www.medscape.com /medline/abstract/1775529 (492 words)

	The Daily Telegraph and Bayer Science Writer Awards
		Colour vision is thought to have evolved in our ancestors about 35 million years ago, giving them more opportunities to find fruit and leaves to eat.
		Each form of iodopsin occurs in a different cone type and the relative stimulation of each type is interpreted by the brain as a particular colour.
		Iodopsin is a pigment that like all proteins is coded for in the DNA of my genes.
	www.science-writer.co.uk /award_winners/16-19_years/2004/winner.html (730 words)

	Bathoiodopsin, a Primary Intermediate of Iodopsin at Physiological Temperature -- Kandori et al. 87 (22): 8908 -- ... (Site not responding. Last check: 2007-10-13)
		Bathoiodopsin, a Primary Intermediate of Iodopsin at Physiological Temperature
		Measurement of the primary photochemical reaction of iodopsin, a chicken red-sensitive cone visual pigment, was carried out at room temperature by using picosecond (ps) laser photolysis.
		Excitation of iodopsin with a ps green pulse (pulse width, 21 ps) caused the instantaneous formation of a bathochromic product, which was stable on a ps time scale.
	intl.pnas.org /cgi/content/short/87/22/8908 (262 words)

	Does the Chromophore's Ring Move after Photoexcitation of Rhodopsin? Biophysical Journal - Find Articles
		The chicken long-wavelength sensitive cone pigment iodopsin is an example of the type where both residues are in their polar form, and that, along with the effect of chloride binding, shifts the spectrum out to 571 nm.
		However, the Lumi product of iodopsin (535 nm) is shifted by a much larger amount, 1510 cm^sup -1^, and to the blue of its initial absorption maximum.
		Such a large shift might also occur if the chloride were to be released when the Lumi intermediate of iodopsin is formed, but this cause is excluded because the gecko pigment has the chloride, but not the binding site shifting residues, and its Lumi shifts just like the nonchloride binding pigments.
	www.24hourscholar.com /p/articles/mi_qa3938/is_200506/ai_n13642523 (932 words)

	Assignment of the vibrational modes of the chromophores of iodopsin and bathoiodopsin: low-temperature fourier ...
		Assignment of the vibrational modes of the chromophores of iodopsin and bathoiodopsin: low-temperature fourier transform infrared spectroscopy of 13C- and 2H-labeled iodopsins.
		To investigate the chromophore structures of iodopsin and its low-temperature photoproducts, we have assigned their vibrational bands in the Fourier transform infrared (FTIR) spectra using iodopsin samples that were reconstituted with a series of (13)C- and deuterium-labeled retinals.
		The large amount of twisting was reduced by removing the chloride ion from the iodopsin, suggesting that this twisting hinders the relaxation of the torsion near C(11) necessary for the transition to the lumi intermediate and thus results in the thermal reversion of the batho intermediate back to the iodopsin.
	www.medscape.com /medline/abstract/16430225 (335 words)

	MIXING LIGHTS AND PAINTS
		Each is made of a large protein molecule that has attached to it a molecule of retinene, a chemical derived from Vitamin A. The protein molecules differ among the four photopigments (3 cone & 1 rod) to make the four absorb best photons of different energies (colors).
		The iodopsin in the "Green" cone absorbs best (photons that have energies equivalent to) 530 nm.
		The two pieces into which the iodopsin is broken, must be put back together before they can absorb another photon.
	www.indiana.edu /~p1013447/dictionary/col_mix.htm (812 words)

	Science.ie - Science News: Life Sciences News (Site not responding. Last check: 2007-10-13)
		In this time humans have managed to put together a colour visual system which I am told is dependant upon three forms of iodopsin, or colour pigments, each responding to light of different wavelengths.
		Each form of iodopsin occurs in a different cone and the relative stimulation of each type is interpreted by the brain as a particular colour.
		Iodopsin has a protein as its backbone which like all proteins is coded for in the genes of my DNA.
	www.science.ie /content/content.asp?section_id=606&language_id=1&publication_id=1840 (1028 words)

	HighBeam Encyclopedia - vision (Site not responding. Last check: 2007-10-13)
		The cones secrete the pigment iodopsin and are most effective in bright light; they alone provide color vision.
		The rods, which secrete a substance called visual purple, or rhodopsin, provide vision in dim light or semidarkness; since rods do not provide color vision, objects in such light appear in shades of gray.
		The iodopsin of cone cells is less sensitive than rhodopsin, and therefore is not activated by weak light, while in bright light the highly sensitive rhodopsin of rod cells breaks down so rapidly that it soon becomes inactive.
	www.encyclopedia.com /html/v/vision.asp (1089 words)

	[No title]
		In this time humans have managed to put together a colour visual system which I am told is dependant upon three forms of iodopsin, or colour pigments, each responding to light of different wavelengths.
		Each form of iodopsin occurs in a different cone and the relative stimulation of each type is interpreted by the brain as a particular colour.
		Iodopsin has a protein as its backbone which like all proteins is coded for in the genes of my DNA.
	www.universityscience.ie /pages/news/2004/RDS_Overall_Winner.doc (1014 words)

	Physiology: Colour Vision (Site not responding. Last check: 2007-10-13)
		There are 3 types of cones, each with a different iodopsin (a photosensitive pigment).
		We cannot see colour in dim light, because the light intensity is not strong enough to stimulate (or bleach) iodopsin.
		The threshold frequency of cones is high and so require more light for stimulation, unlike the stimulation of rhodopsin in rods which requires weaker light.
	library.thinkquest.org /28030/physio/colour.htm (307 words)

	Molecular and biochemical analyses of iodopsin in rd chick retina [published erratum appears in Invest Ophthalmol Vis ...
		Molecular and biochemical analyses of iodopsin in rd chick retina [published erratum appears in Invest Ophthalmol Vis Sci 1994 Jul;35(8):3126]
		iodopsin and transcription of this gene are normal in the rd mutant.
		post-translational processing of iodopsin may be abnormal in this mutant.
	www.iovs.org /cgi/content/abstract/35/5/2550 (408 words)

	Pion abstract
		Opponent rhodopsin receptor in rod and opponent iodopsin receptor in cone to underlie the human colour perception
		The short-wave, middle-wave, and long-wave cone receptors with their spectral curves conventionally chosen from the multitude of vector rotations in the three-dimensional colour space cannot explain some visual phenomena.
		Mathematical simulation of elementary visual stimuli for subject-selective image quality metrics (Gavrik, 1998 Proceedings of the SPIE 3409 12) has detected self-filtering colour-separation facilities of rhodopsin in rods and iodopsin in cones.
	www.perceptionweb.com /abstract.cgi?id=v980277 (340 words)

	Probing for the threshold energy for visual transduction: Red-shifted visual pigment analogs from ...
		While azulenic retinal analogs failed to yield a red-shifted visual pigment analog, the 9-cis isomers of the push-pull polyenals 3-methoxy-3-dehydroretinal and 14F-3-methoxy-3-dehydroretinal yielded iodopsin pigment analogs with absorption maxima at, respectively, 663 and 720 nm.
		The red-cone pigment iodopsin (571 nm), on the other hand, is the most red-shifted natural visual pigment having the retinal chromophore.
		Incorporation of DHR to the opsin moiety of iodopsin, however, forms iodopsin analog (cyanopsin) absorbing maximally at 624 nm (Fig.
	findarticles.com /p/articles/mi_qa3931/is_199907/ai_n8864368 (921 words)

	Ch 18 - The Eye
		In the rods, the molecule is a retinine molecule called neoretinene-b, joined to a protein called an opsin to form rhodopsin.
		The absorption of a photon by the rhodopsin (rod) or the iodopsin (cone) causes the effective rotation of one of the chemical bonds, breaking it loose from the cell membrane and initiating a nerve impulse.
		The rods are, overall, about 5 times more sensitive to light than the cones, so that they tend to be used for night vision (with no color discrimination), while the coned dominate at higher light levels.
	www.physics.uc.edu /~sitko/LightColor/18-EyeStructure/Eye.htm (932 words)

	Rowland Lab - Contact Us
		Larkin, P. and Semple-Rowland, S.L. A null mutation in guanylate cyclase -1 alters the temporal dynamics and light entrainment properties of the iodopsin rhythm in cone photoreceptor cells.
		Larkin, P., Baehr, W., and Semple-Rowland, S.L. Circadian regulation of iodopsin and Clock is disrupted in the retinal degeneration (rd) chicken retina.
		Zhang, Y. and Semple-Rowland, S.L. Circadian regulation of iodopsin expression in the developing retina ---in vitro and in ovo studies.
	www.mbi.ufl.edu /~rowland/circadian.htm (440 words)

	Reference.com/Encyclopedia/Eye
		The process through which these proteins go is quite similar—upon being subjected to electromagnetic radiation of a particular wavelength and intensity, the protein breaks down into two constituent products.
		Rhodopsin, of rods, breaks down into opsin and retinal; iodopsin of cones breaks down into photopsin and retinal.
		Furthermore, color is distinguishable when breaking down the iodopsin of cone cells because there are three forms of this protein.
	www.reference.com /browse/wiki/Eye (4648 words)

	vision. The Columbia Encyclopedia, Sixth Edition. 2001-05
		The rods, which secrete a substance called visual purple, or rhodopsin, provide vision in dim light or semidarkness; since rods do not provide color vision, objects in such light appear in shades of gray.
		The iodopsin of cone cells is less sensitive than rhodopsin, and therefore is not activated by weak light, while in bright light the highly sensitive rhodopsin of rod cells breaks down so rapidly that it soon becomes inactive.
		There is a depression near the center of the retina called the fovea that contains only cone cells.
	www.bartleby.com /65/vi/vision.html (918 words)

	Chromophore Configuration of Iodopsin and Its Photoproducts Formed at Low Temperatures
		The photochemical reactions of iodopsin at low temperatures were investigated by a combination of absorption spectroscopy and chromophore extraction to show the formation of isomeric photoproducts other than the all-trans intermediates.
		We first confirmed that the chromophore in iodopsin is an 11-cis-retinal.
		Next, iodopsin samples were irradiated with light of different wavelengths at selected temperatures ranging from -190 to 0
	pubs.acs.org /cgi-bin/abstract.cgi/bichaw/1996/35/i46/abs/bi9614850.html (370 words)

	Interactive Fly, Drosophila
		mRNA levels of iodopsin and the chicken homolog of Clock (cClock) were compared in the retinas of normal and rd (retinal degeneration) chickens that lack functional rod and cone phototransduction cascades.
		Iodopsin is a circadian-regulated, photoreceptor-specific gene expressed in chicken retina, and Clock is a transcription factor that has been shown to play a role in the circadian clock mechanism in mouse and Drosophila.
		cClock and iodopsin transcript levels undergo daily oscillations in retinas of normal animals housed under 12 h light:12 h dark (12L:12D) conditions, and these oscillations are maintained in the absence of light.
	www.sdbonline.org /fly/neural/clock2.htm (11466 words)

	iodopsin \| Other \| Dictionary & Translation by Babylon
		No results for "iodopsin" were found in Additional
		Photopsins are the photoreceptor pigments found in the cone cells of the retina that are the basis of color vision.
		iodopsin, pigment that is sensitive to light (Chemistry)
	www.babylon.com /definition/iodopsin/Other (145 words)

	Localization of iodopsin in the chick retina during in vivo and in vitro cone differentiation -- Araki et al. 31 (8): ...
		Localization of iodopsin in the chick retina during in vivo and in vitro cone differentiation -- Araki et al.
		Localization of iodopsin in the chick retina during in vivo and in vitro cone differentiation
		pigment, iodopsin, we investigated the localization of iodopsin in the
	www.iovs.org /cgi/content/abstract/31/8/1466 (323 words)

	Chaurasia, Mol Vis 2006; 12:215-223.
		With respect to the latter possibility, it should be noted that gap junction uncoupling agents disrupt circadian expression of Aanat and iodopsin in explant cultures of chick retina [50].
		Circadian regulation of iodopsin gene expression in embryonic photoreceptors in retinal cell culture.
		Circadian regulation of iodopsin and clock is altered in the retinal degeneration chicken retina.
	www.molvis.org /molvis/v12/a24 (4558 words)

	No Slide Title (Site not responding. Last check: 2007-10-13)
		They contain another type of visual pigment called iodopsin.
		There are 3 main types of cone cells in the retina - red, blue and green.
		Each cone cell type contains a slightly different type of iodopsin.
	www.life.sci.qut.edu.au /LSB231/231lect12/231lect12_files/slide0165.htm (95 words)

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