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- W2020685058 abstract "We present a number of theoretical results concerning the properties of and differences amongst several red fluorescent proteins (RFPs). RFPs are an extraordinarily useful group of fluorescent proteins that fluoresce at red-shifted wavelengths compared to GFP, thereby extending the color palette of fluorescent proteins for use in applications like FRET and multi-channel imaging. This redder fluorescence is caused by the extension of the pi-conjugated chain through oxidation of a second backbone bond of either Phenylalanine or Isoleucine, depending on the particular RFP. Our work has focused on the RFPs mCherry, mPlum, and DsRed, which share a common chromophore. Since these RFPs share a chromophore, differences in their photophysical properties must be due to differences in their chromophore environments. We performed a series of 100 ns molecular dynamics simulations followed by ZINDO semi-empirical quantum mechanical calculations in an effort to explore variables such as excitation wavelength, quantum yield, and photostability in these RFPs. The ZINDO calculations were performed on MD simulation frames at 1 ps resolution. This fine resolution allowed for the observation of rare conformational states that suggest reasons for the known differences in quantum yield amongst the proteins. Notably, the electric field contributions from every non-chromophore protein atom and ion, and the ∼14,000 simulation cell water molecules, were used as a perturbation in the ZINDO calculations, which allowed us to query the electrostatic environmental influence on the chromophore." @default.
- W2020685058 created "2016-06-24" @default.
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- W2020685058 date "2013-01-01" @default.
- W2020685058 modified "2023-09-27" @default.
- W2020685058 title "Md+Qm Calculations Explore the Origins of Differences amongst the Red Fluorescent Proteins" @default.
- W2020685058 doi "https://doi.org/10.1016/j.bpj.2012.11.3774" @default.
- W2020685058 hasPublicationYear "2013" @default.
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