Alpha-helices direct excitation energy flow in the Fenna Matthews Olson protein - Wikidata - awgldk - TriplyDB

Alpha-helices direct excitation energy flow in the Fenna Matthews Olson protein

Alpha-helices direct excitation energy flow in the Fenna Matthews Olson protein

http://www.wikidata.org/entity/Q36089118

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Long-lived quantum coherence in photosynthetic complexes at physiological temperature On the Conflicting Estimations of Pigment Site Energies in Photosynthetic Complexes: A Case Study of the CP47 Complex Revisiting the optical properties of the FMO protein Theory of solvatochromic shifts in nonpolar solvents reveals a new spectroscopic rule The feasibility of coherent energy transfer in microtubules.Extracting the excitonic Hamiltonian of the Fenna-Matthews-Olson complex using three-dimensional third-order electronic spectroscopy Electronic resonance with anticorrelated pigment vibrations drives photosynthetic energy transfer outside the adiabatic framework.Spectroscopic properties of reaction center pigments in photosystem II core complexes: revision of the multimer model.Visualization of excitonic structure in the Fenna-Matthews-Olson photosynthetic complex by polarization-dependent two-dimensional electronic spectroscopy Chirality-based signatures of local protein environments in two-dimensional optical spectroscopy of two species photosynthetic complexes of green sulfur bacteria: simulation study.Membrane orientation of the FMO antenna protein from Chlorobaculum tepidum as determined by mass spectrometry-based footprinting.Native mass spectrometry of photosynthetic pigment-protein complexes.Theoretical examination of quantum coherence in a photosynthetic system at physiological temperature Nonlinear network model analysis of vibrational energy transfer and localisation in the Fenna-Matthews-Olson complex.Characterization of an FMO variant of Chlorobaculum tepidum carrying bacteriochlorophyll a esterified by geranylgeraniol.Native electrospray mass spectrometry reveals the nature and stoichiometry of pigments in the FMO photosynthetic antenna protein.Quantum chemical description of absorption properties and excited-state processes in photosynthetic systems.Computational methodologies and physical insights into electronic energy transfer in photosynthetic light-harvesting complexes.Structure-based modeling of energy transfer in photosynthesis.Understanding photosynthetic light-harvesting: a bottom up theoretical approach.A new spectroscopic tool for analyzing excitonic structure and dynamics in pigment-protein complexes.Two-dimensional electronic spectra of the photosynthetic apparatus of green sulfur bacteria.Normal mode analysis of the spectral density of the Fenna-Matthews-Olson light-harvesting protein: how the protein dissipates the excess energy of excitons Revealing the functional states in the active site of BLUF photoreceptors from electrochromic shift calculations.Absence of Selection for Quantum Coherence in the Fenna-Matthews-Olson Complex: A Combined Evolutionary and Excitonic Study.Chemical oxidation of the FMO antenna protein from Chlorobaculum tepidum.Environmental correlation effects on excitation energy transfer in photosynthetic light harvesting.Oxidative species-induced excitonic transport in tubulin aromatic networks: Potential implications for neurodegenerative disease.Metal Cations Induced αβ-BChl a Heterogeneity in LH1 as Revealed by Temperature-Dependent Fluorescence Splitting.Efficient and accurate simulations of two-dimensional electronic photon-echo signals: Illustration for a simple model of the Fenna-Matthews-Olson complex.Structure-based simulation of linear optical spectra of the CP43 core antenna of photosystem II.Constrained geometric dynamics of the Fenna-Matthews-Olson complex: the role of correlated motion in reducing uncertainty in excitation energy transfer.On destabilization of the Fenna-Matthews-Olson complex of Chlorobaculum tepidum.Efficient estimation of energy transfer efficiency in light-harvesting complexes.First-principles calculation of electronic spectra of light-harvesting complex II.The three-dimensional structure of the FMO protein from Pelodictyon phaeum and the implications for energy transfer.Path induced coherent energy transfer in light-harvesting complexes in purple bacteria.The nature of the low energy band of the Fenna-Matthews-Olson complex: vibronic signatures.Controlling the Hydrolysis and Loss of Nitrogen Fertilizer (Urea) by using a Nanocomposite Favors Plant Growth.Local protein solvation drives direct down-conversion in phycobiliprotein PC645 via incoherent vibronic transport.

P2860

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P2860

Alpha-helices direct excitation energy flow in the Fenna Matthews Olson protein

http://www.wikidata.org/entity/Q36089118

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2007 nî lūn-bûn

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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2007年论文

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Alpha-helices direct excitation energy flow in the Fenna Matthews Olson protein

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Alpha-helices direct excitation energy flow in the Fenna Matthews Olson protein

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Alpha-helices direct excitation energy flow in the Fenna Matthews Olson protein

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Alpha-helices direct excitation energy flow in the Fenna Matthews Olson protein

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Alpha-helices direct excitation energy flow in the Fenna Matthews Olson protein

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Alpha-helices direct excitation energy flow in the Fenna Matthews Olson protein

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PNAS.0708222104

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Alpha-helices direct excitation energy flow in the Fenna Matthews Olson protein

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P2093

Ayjamal Abdurahman

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Björn Rabenstein

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Frank Müh

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Julia Adolphs

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Thomas Renger

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P2860

How photosynthetic reaction centers control oxidation power in chlorophyll pairs P680, P700, and P870

How proteins trigger excitation energy transfer in the FMO complex of green sulfur bacteria

Evidence for wavelike energy transfer through quantum coherence in photosynthetic systems

pKa's of ionizable groups in proteins: atomic detail from a continuum electrostatic model

Calculation of electrostatic effects at the amino terminus of an alpha helix.

Crystal structure of the bacteriochlorophyll a protein from Chlorobium tepidum.

The reaction center complex from the green sulfur bacterium Chlorobium tepidum: a structural analysis by scanning transmission electron microscopy.

The role of the alpha-helix dipole in protein function and structure.

Structure and X-ray amino acid sequence of a bacteriochlorophyll A protein from Prosthecochloris aestuarii refined at 1.9 A resolution.

The quantitative relationship between structure and polarized spectroscopy in the FMO complex of Prosthecochloris aestuarii: refining experiments and simulations.

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43

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104

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Hiroshi Ishikita

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2007-10-11T00:00:00Z

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5905544

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