Jump to main content
Jump to site search

Issue 25, 2016
Previous Article Next Article

Chromophore interactions leading to different absorption spectra in mNeptune1 and mCardinal red fluorescent proteins

Author affiliations

Abstract

Extensive MD simulations combined with QM/MM calculations have been performed on mNeptune1 and mCardinal red fluorescent proteins to establish the reasons behind the red shift of the excitation wavelength of mCardinal with respect to mNeptune1. In both cases, it is seen that Arg197 stabilizes the chromophore but cannot be described as stabilizing preferentially the excited state because of the anchor point of the interaction. The interactions of the linking bonds to the α-helix of both proteins to the chromophore have been analyzed. It has been found that, besides the presence of a strategically placed residue Gln41 in mCardinal, solvation water molecules play an active role in the energetics of the stabilization of the excited state, which is preferentially stabilized in the case of mCardinal in contrast to mNeptune1.

Graphical abstract: Chromophore interactions leading to different absorption spectra in mNeptune1 and mCardinal red fluorescent proteins

Back to tab navigation

Supplementary files

Publication details

The article was received on 25 Feb 2016, accepted on 01 Jun 2016 and first published on 02 Jun 2016


Article type: Paper
DOI: 10.1039/C6CP01297C
Citation: Phys. Chem. Chem. Phys., 2016,18, 16964-16976
  •   Request permissions

    Chromophore interactions leading to different absorption spectra in mNeptune1 and mCardinal red fluorescent proteins

    P. Armengol, R. Gelabert, M. Moreno and J. M. Lluch, Phys. Chem. Chem. Phys., 2016, 18, 16964
    DOI: 10.1039/C6CP01297C

Search articles by author

Spotlight

Advertisements