Abstract
Dynamical and luminescent properties of the Green Fluorescent Protein (GFP) are being explored via molecular dynamics (MD) simulations and quantum chemistry calculations with the aim of facilitating the rational development of GFP as a probe for cellular functions. Results from an MD simulation of wild type GFP demonstrate the rigidity of the structural framework of GFP, and a very stable hydrogen bond network around the chromophore. Furthermore, excited state calculations have been performed on the chromophore in vacuum, and we report about our work in progress here.
Original language | English |
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Pages (from-to) | 288-295 |
Number of pages | 8 |
Journal | ACS Symposium Series |
Volume | 712 |
DOIs | |
State | Published - 1998 |
Externally published | Yes |