Chromophores of the green fluorescent protein studied in the gas phase

Autor:	I. B. Nielsen, Ulrik Pedersen, Steen Uttrup Pedersen, Shigeo Tomita, A. Lapierre, Steen Brøndsted Nielsen, Lars H. Andersen
Rok vydání:	2002
Předmět:	chemistry.chemical_classification Absorption spectroscopy Magnetic circular dichroism Chemistry Biomolecule Side chain Protonation Chromophore Absorption (chemistry) Photochemistry Atomic and Molecular Physics and Optics Green fluorescent protein
Zdroj:	The European Physical Journal D. 20:597-600
ISSN:	1434-6079 1434-6060
DOI:	10.1140/epjd/e2002-00141-0
Popis:	Absorption of gas-phase biomolecules has been studied at the heavy-ion storage ring ELISA. Here we discuss the absorption characteristics of the chromophores of the Green Fluorescent Protein (GFP). The gas-phase absorption maximum of the deprotonated chromophore (anion form) is at 479 nm. This is almost identical to one of the two absorption maxima of the protein, being at 477 nm, which is ascribed to a deprotonated chromophore in the protein. The protonated chromophore (cation form) has a maximum at 406 nm in the gas phase. We compare the gas-phase results with absorption profiles of GFP and chromophores in liquids, and argue that the absorption characteristics of GFP are mainly ascribed to intrinsic chemical properties of the chromophore. Evidently, the special β-can structure of GFP provides shielding of the chromophore from the surroundings without significantly changing the electronic structure of the chromophore through interactions with amino acid side chains.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::5eb0b3296ac59d24aca903dabaae9925 https://doi.org/10.1140/epjd/e2002-00141-0 Zobrazit plný text záznamu Full text from SpringerLink