Resonance Raman studies of bathorhodopsin: evidence for a protonated Schiff base linkage.
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Resonance Raman microscopy of rod and cone photoreceptors.Resonance Raman studies of the primary photochemical event in visual pigments.Bathorhodopsin structure in the room-temperature rhodopsin photosequence: picosecond time-resolved coherent anti-Stokes Raman scattering.Vibrational spectrum of the lumi intermediate in the room temperature rhodopsin photo-reaction.Nature of the chromophore binding site of bacteriorhodopsin: the potential role of Arg82 as a principal counterion.Photochemistry of rhodopsin and isorhodopsin investigated on a picosecond time scaleThe nature of the primary photochemical events in rhodopsin and isorhodopsinResonance Raman study of the primary photochemistry of visual pigments. Hypsorhodopsin.Glutamic acid 181 is negatively charged in the bathorhodopsin photointermediate of visual rhodopsin.QM/MM study of the structure, energy storage, and origin of the bathochromic shift in vertebrate and invertebrate bathorhodopsins.Applications of ultrafast laser spectroscopy for the study of biological systems.Resonance Raman spectra of bacteriorhodopsin's primary photoproduct: evidence for a distorted 13-cis retinal chromophore.Near-IR resonance Raman spectroscopy of archaerhodopsin 3: effects of transmembrane potentialGPCR activation: protonation and membrane potentialPhotoisomerization, energy storage, and charge separation: a model for light energy transduction in visual pigments and bacteriorhodopsin.Time-resolved resonance Raman spectroscopy of intermediates of bacteriorhodopsin: The bK(590) intermediate.Microbial and animal rhodopsins: structures, functions, and molecular mechanisms.The visual process: photophysics and photoisomerization of model visual pigments and the primary reaction.Infra-red and Raman spectroscopic studies of enzyme structure and functionThe molecular aspects of visual photoreceptors.Resonance Raman analysis of the mechanism of energy storage and chromophore distortion in the primary visual photoproduct.Low-temperature FTIR spectroscopy provides evidence for protein-bound water molecules in eubacterial light-driven ion pumps.
P2860
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P2860
Resonance Raman studies of bathorhodopsin: evidence for a protonated Schiff base linkage.
description
1979 nî lūn-bûn
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1979年の論文
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1979年学术文章
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1979年学术文章
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1979年学术文章
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1979年学术文章
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1979年学术文章
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1979年學術文章
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1979年學術文章
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1979年學術文章
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name
Resonance Raman studies of bathorhodopsin: evidence for a protonated Schiff base linkage.
@ast
Resonance Raman studies of bathorhodopsin: evidence for a protonated Schiff base linkage.
@en
type
label
Resonance Raman studies of bathorhodopsin: evidence for a protonated Schiff base linkage.
@ast
Resonance Raman studies of bathorhodopsin: evidence for a protonated Schiff base linkage.
@en
prefLabel
Resonance Raman studies of bathorhodopsin: evidence for a protonated Schiff base linkage.
@ast
Resonance Raman studies of bathorhodopsin: evidence for a protonated Schiff base linkage.
@en
P2860
P356
P1476
Resonance Raman studies of bathorhodopsin: evidence for a protonated Schiff base linkage.
@en
P2093
P2860
P356
10.1073/PNAS.76.1.33
P407
P577
1979-01-01T00:00:00Z