Abstract
Paramagnetic probes, whose approach to proteins can be monitored by nuclear magnetic resonance (NMR) studies, have been found of primary relevance for investigating protein surfaces accessibility. Here, paramagnetic probes are also suggested for a systematic investigation on protein aggregation. Bovin pancreatic trypsin inhibitor (BPTI) was used as a model system for aggregation by analyzing its interaction with TEMPOL and Gd(III)DTPA-BMA. Some of the measured paramagnetic relaxation rates of BPTI protons exhibited a reverse dependence on protein concentration, which can be attributed to the formation of transient BPTI aggregates.
| Original language | English |
|---|---|
| Pages (from-to) | 856-862 |
| Number of pages | 7 |
| Journal | Biochimica et Biophysica Acta - Proteins and Proteomics |
| Volume | 1764 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - May 2006 |
Keywords
- BPTI
- Gd(III)DTPA-BMA
- NMR
- Paramagnetic probe
- Protein aggregation
- Surface accessibility
- TEMPOL
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