FTIR spectroscopy of complexes formed between metarhodopsin II and C-terminal peptides from the G-protein alpha- and gamma-subunits.
FEBS Lett
; 473(2): 259-64, 2000 May 12.
Article
em En
| MEDLINE
| ID: mdl-10812086
ABSTRACT
Metarhodopsin II (MII) provides the active conformation of rhodopsin for interaction with the G-protein, Gt. Fourier transform infrared spectra from samples prepared by centrifugation reflect the pH dependent equilibrium between MII and inactive metarhodopsin I. C-terminal synthetic peptides (Gtalpha(340-350) and Gtgamma(60-71)farnesyl) stabilize MII. We find that both peptides cause similar spectral changes not seen with control peptides (Gtalpha (K341R, L349A) and non-farnesylated Gtgamma). The spectra reflect all the protonation dependent bands normally observed when MII is formed at acidic pH. Beside the protonation dependent bands, additional features, similar with both peptides, appear in the amide I and II regions.
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Base de dados:
MEDLINE
Assunto principal:
Rodopsina
/
Espectroscopia de Infravermelho com Transformada de Fourier
/
Proteínas Heterotriméricas de Ligação ao GTP
Limite:
Animals
Idioma:
En
Ano de publicação:
2000
Tipo de documento:
Article