Properties of the emitting state of the green fluorescent protein resolved at the CASPT2//CASSCF/CHARMM level.
A "brute-force" ab initio CASPT2//CASSCF/CHARMM computational approach is employed to investigate the properties of the emitting state of the wild-type green fluorescence protein. The results indicate that the emitting moiety corresponds to a slightly perturbed H2O- - -chromophore complex. Thus, the protein matrix seems to be designed in such a way to mimic an environment that is more similar to gas-phase than water solution.
Sinicropi
Adalgisa
A
Dipartimento di Chimica, Università di Siena, via Aldo Moro I-53100 Siena, Italy.
Andruniow
Tadeusz
T
Ferré
Nicolas
N
Basosi
Riccardo
R
Olivucci
Massimo
M
D018360:Crystallography, X-Ray; D049452:Green Fluorescent Proteins / Q000737:chemistry*; D049449:Luminescence; D008956:Models, Chemical; D008958:Models, Molecular; D011789:Quantum Theory; D013816:Thermodynamics
D049452:Green Fluorescent Proteins