We report on the folding properties of the protein azurin, deposited onto SiO2 surfaces and subsequently dehydrated. The molecular films have been maintained at ambient conditions through several days, and the ageing effects have been investigated by fluorescence spectroscopy. The experimental results show a modest initial conformational rearrangement, followed by long-term stability. Interestingly, upon rehydration of the biomolecular films at the end of the investigated period (approximately one month), azurin returns to exhibit a native-like conformation. This study indicates a rather surprising resilience of proteins to ambient conditions and sheds a somewhat unexpected positive light on reliability in biomolecular electronics
Ageing of solid-state protein films: Behavior of azurin at ambient conditions
Maruccio G;Del Mercato L L;
2005
Abstract
We report on the folding properties of the protein azurin, deposited onto SiO2 surfaces and subsequently dehydrated. The molecular films have been maintained at ambient conditions through several days, and the ageing effects have been investigated by fluorescence spectroscopy. The experimental results show a modest initial conformational rearrangement, followed by long-term stability. Interestingly, upon rehydration of the biomolecular films at the end of the investigated period (approximately one month), azurin returns to exhibit a native-like conformation. This study indicates a rather surprising resilience of proteins to ambient conditions and sheds a somewhat unexpected positive light on reliability in biomolecular electronicsI documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
