Time-resolved methods in biophysics. 8. Frequency domain fluorometry: applications to intrinsic protein fluorescence.
Photochem Photobiol Sci
; 7(11): 1301-12, 2008 Nov.
Article
en En
| MEDLINE
| ID: mdl-18958316
ABSTRACT
Time-resolved fluorescence spectroscopy is an indispensable tool in the chemical, physical and biological sciences for the study of fast kinetic processes in the subpicosecond to microsecond time scale. This review focuses on the development and modern implementation of the frequency domain approach to time-resolved fluorescence. Both intensity decay (lifetime) and anisotropy decay (dynamic polarization) will be considered and their application to intrinsic protein fluorescence will be highlighted. In particular we shall discuss the photophysics of the aromatic amino acids, tryptophan, tyrosine and phenylalanine, which are responsible for intrinsic protein fluorescence. This discussion will be illustrated with examples of frequency domain studies on several protein systems.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Biofisica
/
Proteínas
/
Fluorescencia
/
Fluorometría
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Photochem Photobiol Sci
Asunto de la revista:
BIOLOGIA
/
QUIMICA
Año:
2008
Tipo del documento:
Article
País de afiliación:
Estados Unidos
Pais de publicación:
ENGLAND
/
ESCOCIA
/
GB
/
GREAT BRITAIN
/
INGLATERRA
/
REINO UNIDO
/
SCOTLAND
/
UK
/
UNITED KINGDOM