Published in Proc Natl Acad Sci U S A on July 01, 1982
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Resonance Raman studies of the primary photochemical event in visual pigments. Biophys J (1980) 1.33
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Resonance Raman study of the primary photochemistry of bacteriorhodopsin. Proc Natl Acad Sci U S A (1981) 1.17
On the origin of the red emission of light adapted purple membrane of Halobacterium halobium. FEBS Lett (1977) 1.15
Resonance Raman spectroscopy of specifically [epsilon-15N]lysine-labeled bacteriorhodopsin. Proc Natl Acad Sci U S A (1981) 1.11
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Millisecond Fourier-transform infrared difference spectra of bacteriorhodopsin's M412 photoproduct. Proc Natl Acad Sci U S A (1987) 1.74
Protein dynamics in the bacteriorhodopsin photocycle: submillisecond Fourier transform infrared spectra of the L, M, and N photointermediates. Proc Natl Acad Sci U S A (1991) 1.71
Replacement of leucine-93 by alanine or threonine slows down the decay of the N and O intermediates in the photocycle of bacteriorhodopsin: implications for proton uptake and 13-cis-retinal----all-trans-retinal reisomerization. Proc Natl Acad Sci U S A (1991) 1.69
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Photocleavable biotin derivatives: a versatile approach for the isolation of biomolecules. Proc Natl Acad Sci U S A (1995) 1.50
A spectroscopic study of rhodopsin alpha-helix orientation. Biophys J (1980) 1.45
Evidence for a tyrosine protonation change during the primary phototransition of bacteriorhodopsin at low temperature. Proc Natl Acad Sci U S A (1986) 1.39
A biophysical study of integral membrane protein folding. Biochemistry (1997) 1.35
Fourier transform infrared difference spectra of intermediates in rhodopsin bleaching. Science (1983) 1.33
Anomalous amide I infrared absorption of purple membrane. Science (1979) 1.24
Fourier transform infrared evidence for Schiff base alteration in the first step of the bacteriorhodopsin photocycle. Biochemistry (1984) 1.23
The reaction of hydroxylamine with bacteriorhodopsin studied with mutants that have altered photocycles: selective reactivity of different photointermediates. Proc Natl Acad Sci U S A (1991) 1.17
Tyrosine and carboxyl protonation changes in the bacteriorhodopsin photocycle. 1. M412 and L550 intermediates. Biochemistry (1987) 1.17
The Schiff base counterion of bacteriorhodopsin is protonated in sensory rhodopsin I: spectroscopic and functional characterization of the mutated proteins D76N and D76A. Biochemistry (1994) 1.16
Fourier transform infrared spectroscopy and site-directed isotope labeling as a probe of local secondary structure in the transmembrane domain of phospholamban. Biophys J (1996) 1.16
Time-resolved Fourier transform infrared spectroscopy of the bacteriorhodopsin mutant Tyr-185-->Phe: Asp-96 reprotonates during O formation; Asp-85 and Asp-212 deprotonate during O decay. Photochem Photobiol (1992) 1.16
Vibrational spectroscopy of bacteriorhodopsin mutants. Evidence that ASP-96 deprotonates during the M----N transition. J Biol Chem (1991) 1.15
Resonance Raman spectroscopy of specifically [epsilon-15N]lysine-labeled bacteriorhodopsin. Proc Natl Acad Sci U S A (1981) 1.11
Opsin structure probed by raman spectroscopy of photoreceptor membranes. Science (1976) 1.11
Asp76 is the Schiff base counterion and proton acceptor in the proton-translocating form of sensory rhodopsin I. Biochemistry (1996) 1.10
Detection of a water molecule in the active-site of bacteriorhodopsin: hydrogen bonding changes during the primary photoreaction. Biochemistry (1994) 1.07
Polarized Fourier transform infrared spectroscopy of bacteriorhodopsin. Transmembrane alpha helices are resistant to hydrogen/deuterium exchange. Biophys J (1990) 1.07
Fourier transform infrared spectroscopic evidence for the existence of two conformations of the bacteriorhodopsin primary photoproduct at low temperature. Biochim Biophys Acta (1985) 1.06
Photocleavable biotin phosphoramidite for 5'-end-labeling, affinity purification and phosphorylation of synthetic oligonucleotides. Nucleic Acids Res (1996) 1.06
Substitution of membrane-embedded aspartic acids in bacteriorhodopsin causes specific changes in different steps of the photochemical cycle. Biochemistry (1989) 1.03
Ultraviolet-visible transient spectroscopy of bacteriorhodopsin mutants. Evidence for two forms of tyrosine-185----phenylalanine. J Biol Chem (1990) 1.02
Incorporation of photoreceptor membrane into a multilamellar film. Biophys J (1980) 1.01
Tyrosine protonation changes in bacteriorhodopsin. A Fourier transform infrared study of BR548 and its primary photoproduct. J Biol Chem (1988) 1.01
FTIR analysis of the SII540 intermediate of sensory rhodopsin II: Asp73 is the Schiff base proton acceptor. Biochemistry (2000) 1.01
Primary photochemistry of bacteriorhodopsin: comparison of Fourier transform infrared difference spectra with resonance Raman spectra. Photochem Photobiol (1984) 1.00
Photoexcitation of rhodopsin: conformation changes in the chromophore, protein and associated lipids as determined by FTIR difference spectroscopy. Photochem Photobiol (1988) 1.00
Conformational changes in bacteriorhodopsin studied by infrared attenuated total reflection. Biophys J (1987) 0.99
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Fourier transform infrared difference spectroscopy of rhodopsin mutants: light activation of rhodopsin causes hydrogen-bonding change in residue aspartic acid-83 during meta II formation. Biochemistry (1993) 0.97
Effects of amino acid substitutions in the F helix of bacteriorhodopsin. Low temperature ultraviolet/visible difference spectroscopy. J Biol Chem (1988) 0.95
Fourier transform infrared evidence for a predominantly alpha-helical structure of the membrane bound channel forming COOH-terminal peptide of colicin E1. Biophys J (1991) 0.95
Carboxyl group involvement in the meta I and meta II stages in rhodopsin bleaching. A Fourier transform infrared spectroscopic study. Biochim Biophys Acta (1985) 0.95
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Evidence for rhodopsin refolding during the decay of Meta II. Biophys J (1987) 0.94
Photocleavable peptide-DNA conjugates: synthesis and applications to DNA analysis using MALDI-MS. Nucleic Acids Res (1999) 0.94
Conformational changes in the core structure of bacteriorhodopsin. Biochemistry (1998) 0.93
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Uv-visible spectroscopy of bacteriorhodopsin mutants: substitution of Arg-82, Asp-85, Tyr-185, and Asp-212 results in abnormal light-dark adaptation. Proc Natl Acad Sci U S A (1990) 0.91
Photoactivation of rhodopsin causes an increased hydrogen-deuterium exchange of buried peptide groups. Biophys J (1998) 0.90
Fourier transform Raman spectroscopy of the bacteriorhodopsin mutant Tyr-185-->Phe: formation of a stable O-like species during light adaptation and detection of its transient N-like photoproduct. Biochemistry (1993) 0.90
Photocleavable aminotag phosphoramidites for 5'-termini DNA/RNA labeling. Nucleic Acids Res (1998) 0.89
Hydrogen bonding interactions with the Schiff base of bacteriorhodopsin. Resonance Raman spectroscopy of the mutants D85N and D85A. J Biol Chem (1993) 0.89
Photoactivation of rhodopsin involves alterations in cysteine side chains: detection of an S-H band in the Meta I-->Meta II FTIR difference spectrum. Biophys J (1994) 0.89
The site of attachment of retinal in bacteriorhodopsin. A resonance Raman study. J Biol Chem (1982) 0.88
Substitution of amino acids in helix F of bacteriorhodopsin: effects on the photochemical cycle. Biochemistry (1989) 0.88
Cell-free synthesis, functional refolding, and spectroscopic characterization of bacteriorhodopsin, an integral membrane protein. Biochemistry (1993) 0.87
Spectroscopic study of photoreceptor membrane incorporated into a multilamellar film. Biochem Biophys Res Commun (1980) 0.87
X-ray diffraction and electron microscope study of phase separation in rod outer segment photoreceptor membrane multilayers. Biophys J (1982) 0.87
Tyrosine and carboxyl protonation changes in the bacteriorhodopsin photocycle. 2. Tyrosines-26 and -64. Biochemistry (1987) 0.86
Fourier transform infrared study of photoreceptor membrane. I. Group assignments based on rhodopsin delipidation and reconstitution. Biochim Biophys Acta (1980) 0.86
Tyrosine structural changes detected during the photoactivation of rhodopsin. J Biol Chem (1998) 0.86
Site-directed isotope labeling and ATR-FTIR difference spectroscopy of bacteriorhodopsin: the peptide carbonyl group of Tyr 185 is structurally active during the bR-->N transition. Biochemistry (1995) 0.86
Fourier transform infrared difference spectroscopy of the nicotinic acetylcholine receptor: evidence for specific protein structural changes upon desensitization. Biochemistry (1993) 0.86
Raman spectroscopic investigation of gramicidin A' conformations. Science (1974) 0.86
Protein conformational changes during the bacteriorhodopsin photocycle. A Fourier transform infrared/resonance Raman study of the alkaline form of the mutant Asp-85-->Asn. J Biol Chem (1995) 0.85
Static and time-resolved absorption spectroscopy of the bacteriorhodopsin mutant Tyr-185-->Phe: evidence for an equilibrium between bR570 and an O-like species. Biochemistry (1993) 0.85
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FTIR difference spectroscopy of the bacteriorhodopsin mutant Tyr-185-->Phe: detection of a stable O-like species and characterization of its photocycle at low temperature. Biochemistry (1993) 0.83
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