Denaturation and Renaturation of Self-Assembled Yeast Iso-1-cytochrome c on Au
- 9 March 2004
- journal article
- research article
- Published by American Chemical Society (ACS) in Analytical Chemistry
- Vol. 76 (7) , 2112-2117
- https://doi.org/10.1021/ac035416k
Abstract
We have made surface plasmon resonance (SPR) measurements of yeast iso-1-cytochrome c (Cyt c) on a gold surface. Angle-resolved SPR curves are recorded as a function of urea concentration before and after self-assembly of the Cyt c. Exposure to a urea solution causes denaturation of Cyt c, which shifts the minimum in the SPR curve to a larger angle and decreases the signal amplitude. The Gibbs free energy change for denaturation of the protein on Au is calculated from the change of the SPR signal amplitude with urea concentration. We find that (1) Cyt c can be reversibly denatured and renatured, depending on the urea concentration, and (2) the Gibbs free energy change for denaturation of Cyt c on Au surface in water, ΔG°water, is 1.5 kcal/mol, which is ∼4 times less than that in bulk solution.Keywords
This publication has 19 references indexed in Scilit:
- Comparative Thermodynamic Analysis of DNA−Protein Interactions Using Surface Plasmon Resonance and Fluorescence Correlation SpectroscopyBiochemistry, 2003
- Preparation of a Branched DNA Self-Assembled Monolayer toward Sensitive DNA BiosensorsNano Letters, 2003
- Enzyme-Coated Carbon Nanotubes as Single-Molecule BiosensorsNano Letters, 2003
- Refolding kinetics of cytochrome c551 reveals a mechanistic difference between urea and guanidineProtein Science, 2001
- A pH-Jump Reaction Studied by the Transient Grating Method: Photodissociation ofo-NitrobenzaldehydeThe Journal of Physical Chemistry A, 2000
- Anisotropic Orientation of Horseradish Peroxidase by Reconstitution on a Thiol-Modified Gold ElectrodeChemistry – A European Journal, 2000
- Protein Stability: Functional Dependence of Denaturational Gibbs Energy on Urea ConcentrationBiochemistry, 1999
- Nanoencapsulation of Cytochrome c and Horseradish Peroxidase at the Galleries of α-Zirconium PhosphateChemistry of Materials, 1997
- Conformational changes in adsorbed proteinsLangmuir, 1995
- High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochromes cJournal of Molecular Biology, 1990