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Requirement of Rigid-Body Motion of Transmembrane Helices for Light Activation of Rhodopsin
Conformational changes are thought to underlie the activation of heterotrimeric GTP-binding protein (G protein)—coupled receptors. Such changes in rhodopsin were explored by construction of doubleExpand
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Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S
An HEK293S cell line resistant to ricin was prepared by mutagenesis by using ethyl methanesulfonate. It was shown to lack N-acetylglucosaminyltransferase I (GnTI) activity, and consequently unable toExpand
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Rhodopsin structure, dynamics, and activation: a perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking.
Publisher Summary This chapter presents rhodopsin structure and dynamics at the cytoplasmic face in solution, the comparison between the solution structure and the crystal structure, and theExpand
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Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin.
The characteristic wavelength at which a visual pigment absorbs light is regulated by interactions between protein (opsin) and retinylidene Schiff base chromophore. By using site-directedExpand
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A collision gradient method to determine the immersion depth of nitroxides in lipid bilayers: application to spin-labeled mutants of bacteriorhodopsin.
Ten mutants of bacteriorhodopsin, each containing a single cysteine residue regularly spaced along helix D and facing the lipid bilayer, were derivatized with a nitroxide spin label. Collision ratesExpand
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Transmembrane protein structure: spin labeling of bacteriorhodopsin mutants.
Transmembrane proteins serve important biological functions, yet precise information on their secondary and tertiary structure is very limited. The boundaries and structures of membrane-embeddedExpand
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Identification of core amino acids stabilizing rhodopsin.
Rhodopsin is the only G protein-coupled receptor (GPCR) whose 3D structure is known; therefore, it serves as a prototype for studies of the GPCR family of proteins. Rhodopsin dysfunction has beenExpand
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Cysteine residues 110 and 187 are essential for the formation of correct structure in bovine rhodopsin.
To investigate the role of different cysteine residues in bovine rhodopsin, a series of mutants were prepared in which the cysteine residues were systematically replaced by serines. The mutant genesExpand
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Denaturation and renaturation of bacteriorhodopsin in detergents and lipid-detergent mixtures.
The denatured and renatured states of bacteriorhodopsin have been studied in detergents and lipid/detergent mixtures by using ultraviolet and visible light absorption spectroscopy, fluorescenceExpand
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Structure and function in rhodopsin: A tetracycline-inducible system in stable mammalian cell lines for high-level expression of opsin mutants
Tetracycline-inducible HEK293S stable cell lines have been prepared that express high levels (up to 10 mg/liter) of WT opsin and its mutants only in response to the addition of tetracycline andExpand
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