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| Content Provider | Springer Nature Link |
|---|---|
| Author | Vetri, Valeria Librizzi, Fabio Leone, Maurizio Militello, Valeria |
| Copyright Year | 2007 |
| Abstract | We report here a study on thermal aggregation of BSA at two different pH values selected to be close to the isoelectric point (pI) of this protein. Our aim is to better understand the several steps and mechanisms accompanying the aggregation process. For this purpose we have performed kinetics of integrated intensity emission of intrinsic and extrinsic dyes, tryptophans and ANS respectively, kinetics of Rayleigh scattering and of turbidity. The results confirm the important role played by conformational changes in the tertiary structure, especially in the exposure of internal hydrophobic regions that promote intermolecular interactions. We also confirm that the absence of electrostatic repulsion favours the disordered non-specific interactions between molecules and consequently affects the aggregation rate. Finally, the comparison between BSA and another relative protein, HSA, allows us to clarify the role of different domains involved in the aggregation process. |
| Starting Page | 717 |
| Ending Page | 725 |
| Page Count | 9 |
| File Format | |
| ISSN | 01757571 |
| Journal | European Biophysics Journal |
| Volume Number | 36 |
| Issue Number | 7 |
| e-ISSN | 14321017 |
| Language | English |
| Publisher | Springer-Verlag |
| Publisher Date | 2007-07-12 |
| Publisher Place | Berlin, Heidelberg |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Neurobiology Animal Physiology Plant Physiology Biochemistry Cell Biology Biophysics/Biomedical Physics |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Biophysics |
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