We determined the conditions under which surface plasmon resonance can be used to monitor at real-time the Ca 2+-induced conformational transitions of the sensor protein recoverin immobilized over a sensor chip. The equilibrium and the kinetics of conformational transitions were detected and quantified over a physiological range of Ca 2+ and protein concentrations similar to those found within cells. Structural analysis suggests that the detection principle reflects changes in the hydrodynamic properties of the protein and is not due to a mass effect. The phenomenon appears to be related to changes in the refractive index at the metal/dielectric interface.

Quantitative detection of conformational transitions in a calcium sensor protein by surface plasmon resonance.

DELL'ORCO, Daniele;
2010-01-01

Abstract

We determined the conditions under which surface plasmon resonance can be used to monitor at real-time the Ca 2+-induced conformational transitions of the sensor protein recoverin immobilized over a sensor chip. The equilibrium and the kinetics of conformational transitions were detected and quantified over a physiological range of Ca 2+ and protein concentrations similar to those found within cells. Structural analysis suggests that the detection principle reflects changes in the hydrodynamic properties of the protein and is not due to a mass effect. The phenomenon appears to be related to changes in the refractive index at the metal/dielectric interface.
2010
surface plasmon resonance; calcium binding proteins; kinetics; calcium sensors
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11562/384838
Citazioni
  • ???jsp.display-item.citation.pmc??? 12
  • Scopus 33
  • ???jsp.display-item.citation.isi??? 34
social impact