Replacement of highly conserved E222 by the photostable non-photoconvertible histidine in GFP.
Chembiochem
; 15(10): 1404-8, 2014 Jul 07.
Article
em En
| MEDLINE
| ID: mdl-24919579
ABSTRACT
The widely used green fluorescent protein (GFP) decarboxylates upon irradiation; this involves removal of the acidic function of the glutamic acid at position 222, thereby resulting in the irreversible photoconversion of GFP. To suppress this phenomenon, the photostable, non-photoconvertible histidine was introduced at position 222 in GFP. The variant E222H shows negligible photodynamic processes and high expression yield. In addition, the stable and bright fluorescence over a wide pH range makes the E222H protein an alternative for GFP in fluorescence imaging and spectroscopy. Other fluorescent proteins are predicted to benefit from replacement of the catalytic glutamic acid by histidine.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Fluorescência Verde
/
Substâncias Luminescentes
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
Chembiochem
Assunto da revista:
BIOQUIMICA
Ano de publicação:
2014
Tipo de documento:
Article