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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Characterization of surface-confined alpha-synuclein by surface plasmon resonance measurements.

Urea-driven denaturation and renaturation of surface-bound alpha-synuclein are monitored by surface plasmon resonance (SPR) spectroscopy. The differential SPR angle shift ( Delta Theta(SPR))(Net) enables us to estimate the Gibbs free energy change (DeltaG(o)) for the denaturation of the supported alpha-synuclein. DeltaG(o) for the denaturation of the supported alpha-synuclein, which is indirectly related to its biological activity can be increased significantly by the mixed self-assembled monolayers of 11-mercaptoundecanoic acid and 1,6-hexanedithiol. These SPR measurements of surface-bound biomolecules suggested herein can be further utilized to design effective biological scaffold for biosensor, biocatalyst, and possible diagnosis.[1]

References

  1. Characterization of surface-confined alpha-synuclein by surface plasmon resonance measurements. Kang, T., Hong, S., Kim, H.J., Moon, J., Oh, S., Paik, S.R., Yi, J. Langmuir : the ACS journal of surfaces and colloids. (2006) [Pubmed]
 
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