Imaging protein molecules using FRET and FLIM microscopy.
Curr Opin Biotechnol
; 16(1): 19-27, 2005 Feb.
Article
em En
| MEDLINE
| ID: mdl-15722011
ABSTRACT
Förster (or fluorescence) resonance energy transfer (FRET) and fluorescence lifetime imaging (FLIM) have moved center stage and are increasingly forming part of multifaceted imaging approaches. They are complementary methodologies that can be applied to advanced quantitative analyses. The widening application of FRET and FLIM has been driven by the availability of suitable fluorophores, increasingly sophisticated microscopy systems, methodologies to correct spectral bleed-through, and the ease with which FRET can be combined with other techniques. FRET and FLIM have recently found use in several applications in the analysis of protein-protein interactions with high spatial and temporal specificity (e.g. clustering), in the study of conformational changes, in the analysis of binding sequences, and in applications such as high-throughput screening.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Espectrometria de Fluorescência
/
Proteínas
/
Mapeamento de Interação de Proteínas
/
Transferência Ressonante de Energia de Fluorescência
/
Microscopia de Fluorescência por Excitação Multifotônica
Idioma:
En
Revista:
Curr Opin Biotechnol
Assunto da revista:
BIOTECNOLOGIA
Ano de publicação:
2005
Tipo de documento:
Article
País de afiliação:
Estados Unidos