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2011-Sustainable Industrial Processing Summit
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Editors: | Florian K |
Publisher: | Flogen Star OUTREACH |
Publication Year: | 2012 |
Pages: | 630 pages |
ISBN: | 978-0-9879917-2-0 |
ISSN: | 2291-1227 (Metals and Materials Processing in a Clean Environment Series) |
Green fluorescence protein (GFP) consists of 238 peptides, which is shaped into a barrel structure with a fluorophore inside the barrel. The fluorophore is a tripeptide of Ser-Tyr-Gly, which is rearranged into 4-(p-hydroxybenzylidene)-5-imidazolinone (p-HBI) after folding and autocatalytic reaction. The wild-type GFP has excited-state proton transfer, which causes fluorescence emission a bathchromic shift. This natural phenomenon inspired me to calculate properties of ground-state GFP ionic liquid and excited-states GFP ionic liquid.We used density function theory (DFT) to optimize geometric and electronic structures of ground-state and excited-state GFP, respectively. Mullican charge distribution was used to analyze charge/electron distribution of ground-state and excited-state GFP. The charge/electron distribution make a significant contribution to the solvation properties of the ground-state and excited-state GFP.