Under particular conditions proteins spontaneously aggregate into well-ordered structures called amyloid fibrils. The full elucidation of the fibrillation process requires the identification by biophysical techniques of the conformational and oligomeric species populated during the aggregation mechanism.
(2011). The aggregation mechanisms of amyloid proteins studied by mass spectrometry and other biophysical techniques. (Tesi di dottorato, Università degli Studi di Milano-Bicocca, 2011).
The aggregation mechanisms of amyloid proteins studied by mass spectrometry and other biophysical techniques
SANTAMBROGIO, CARLO
2011
Abstract
Under particular conditions proteins spontaneously aggregate into well-ordered structures called amyloid fibrils. The full elucidation of the fibrillation process requires the identification by biophysical techniques of the conformational and oligomeric species populated during the aggregation mechanism.
File in questo prodotto:
| File | Dimensione | Formato | |
|---|---|---|---|
|
phd_unimib_035738.pdf
accesso aperto
Tipologia di allegato:
Doctoral thesis
Dimensione
2.59 MB
Formato
Adobe PDF
|
2.59 MB | Adobe PDF | Visualizza/Apri |
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
