Abstract
Amyloid fibrils associated with numerous degenerative diseases are non-crystalline and insoluble, and thus are not amenable to conventional X-ray crystallography and solution NMR, the classical tools of structural biology. We have recently demonstrated that deep UV resonance Raman (DUVRR) spectroscopy combined with hydrogen-deuterium exchange and advanced statistical analysis, 2D correlation in particular, allow for quantitative characterization of protein structural evolution at all stages of fibrillation in vitro. The application of DUVRR spectroscopy for studying the fibrillation of lysozyme is briefly overviewed here.
| Original language | English |
|---|---|
| Pages (from-to) | 180-185 |
| Number of pages | 6 |
| Journal | Current Science |
| Volume | 97 |
| Issue number | 2 |
| State | Published - Jul 2009 |
Keywords
- Amyloid fibril
- Chemometrics
- Protein structure
- Raman spectroscopy
- Two-dimensional correlation spectroscopy
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