TY  - JOUR
AU  - Gonçalves, Marcos Brown
AU  - Dreyer, Jens
AU  - Lupieri, Paola
AU  - Barrera-Patiño, Claudia
AU  - Ippoliti, Emiliano
AU  - Webb, Martin R.
AU  - Corrie, John E. T.
AU  - Carloni, Paolo
TI  - Structural prediction of a rhodamine-based biosensor and comparison with biophysical data
JO  - Physical chemistry, chemical physics
VL  - 15
IS  - 6
SN  - 1463-9084
CY  - Cambridge
PB  - RSC Publ.
M1  - FZJ-2015-03618
SP  - 2177 - 2183
PY  - 2013
AB  - The predicted structure has been calculated for a protein-based biosensor for inorganic phosphate (Pi), previously developed by some of us (Okoh et al., Biochemistry, 2006, 45, 14764). This is the phosphate binding protein from Escherichia coli labelled with two rhodamine fluorophores. Classical molecular dynamics and hybrid Car–Parrinello/molecular mechanics simulations allow us to provide molecular models of the biosensor both in the presence and in the absence of Pi. In the latter case, the rhodamine fluorophores maintain a stacked conformation in a ‘face A to face B’ orientation, which is different from the ‘face A to face A’ stacked orientation of free fluorophores in aqueous solution (Ilich et al., Spectrochim. Acta, Part A, 1996, 52, 1323). A protein conformation change upon binding Pi prevents significant stacking of the two rhodamines. In both states, the rhodamine fluorophores form hydrophobic contact with LEU291, without establishing significant hydrogen bonds with the protein. The accuracy of the models is established by a comparison between calculated and experimentalabsorption and circular dichroism spectra.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000313566300050
C6  - pmid:23247608
DO  - DOI:10.1039/C2CP42396K
UR  - https://juser.fz-juelich.de/record/201313
ER  -