| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1178417 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2007 | 8 Pages |
Abstract
The present study demonstrates that H2O2 and OH cause fibril aggregation and catalytic inactivation of porcine fumarase. In the aggregated (oxidized) enzyme, modifications in both secondary and tertiary protein structure occur and the enzyme aggregation obeys to fractal geometry. We then collected information on the fractal dimension and on the size and shape of fumarase aggregates by using Synchrotron Radiation (SR) Small Angle X-ray Scattering (SAXS) analysis. The geometrical self-similarity assessment of aggregates has been revealed by both AFM and SEM measurements at different scale of magnification. Micrographs collected remarkably demonstrate that the oxidized enzyme shows dendritic fractal structure over a large range of sizes.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Mario Barteri, Carlo Coluzza, Simona Rotella,