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The Gas-Phase Absorption Spectrum of a Neutral GFP Model Chromophore

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TLDR
There is strong experimental evidence that, in terms of absorption, the conditions in the hydrophobic interior of this protein are very close to those in vacuum, and the absorption of GFP is primarily determined by intrinsic chromophore properties.
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This article is published in Biophysical Journal.The article was published on 2007-01-01 and is currently open access. It has received 52 citations till now. The article focuses on the topics: Chromophore & Green fluorescent protein.

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Photodynamics in complex environments: ab initio multiple spawning quantum mechanical/molecular mechanical dynamics.

TL;DR: An overview of the full multiple spawning method for multistate quantum dynamics, together with hybrid quantum mechanical/molecular mechanical potential energy surfaces using both semiempirical and ab initio QM methods, and a comparison of the excited-state dynamics of several biological chromophores in solvent and protein environments are presented.
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Absorption Spectrum of the Green Fluorescent Protein Chromophore: A Difficult Case for ab Initio Methods?

TL;DR: A thorough comparative investigation of the excitation energies of the anionic and neutral forms of the green fluorescent protein (GFP) chromophore in the gas phase using a variety of first-principle theoretical approaches commonly used to access excited state properties of photoactive molecules finds that all approaches give roughly the same vertical excitation, while TDDFT predicts an excitation for the neutral Chromophore significantly lower than the highly correlated methods.
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Potential Energy Landscape of the Electronic States of the GFP Chromophore in Different Protonation Forms: Electronic Transition Energies and Conical Intersections.

TL;DR: The results reproduce essential features of previous ab initio calculations of the anionic form of the chromophore and provide an extension for the neutral, cationic, and zwitterionic forms, which are important in the protein environment.
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Activation and tuning of green fluorescent protein chromophore emission by alkyl substituent-mediated crystal packing.

TL;DR: Three-dimensional steady-state and time-resolved emission spectroscopies in the solid state, as well as single-crystal X-ray diffraction, reveal the nature of complex emission in the crystals.
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Modeling the Excited States of Biological Chromophores within Many-Body Green’s Function Theory

TL;DR: First-principle many-body Green's function theory bridges the gap between time-dependent density functional theory and high-level quantum chemistry methods, combining the efficiency of the former with the accuracy of the latter, making MBGFT a promising method for studying excitations in complex biological systems.
References
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Journal ArticleDOI

The green fluorescent protein

TL;DR: In just three years, the green fluorescent protein from the jellyfish Aequorea victoria has vaulted from obscurity to become one of the most widely studied and exploited proteins in biochemistry and cell biology.
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Crystal structure of the Aequorea victoria green fluorescent protein.

TL;DR: The green fluorescent protein (GFP) from the Pacific Northwest jellyfish Aequorea victoria has generated intense interest as a marker for gene expression and localization of gene products.
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The Molecular Basis of Visual Excitation

TL;DR: The article that follows consists of most of the lecture delivered by Professor Wald last December when he received the Nobel Prize for Medicine in Stockholm.
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Molecular Basis of Visual Excitation

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