Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2052697 | FEBS Letters | 2005 | 4 Pages |
Abstract
The aggregation of a recombinant lipase as inclusion bodies (IBs) was studied directly within intact Escherichia coli cells by FT-IR microspectroscopy. Through this approach, it was possible to monitor in real time the different kinetics of IB formation at 37 and 27 °C, in excellent agreement with the results of the SDS–PAGE analysis. Furthermore, insights on the residual native-like structure of the expressed protein within IB – both isolated and inside cells – were obtained by the secondary structure analysis of the Amide I band in the IB FT-IR spectra.
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Authors
Diletta Ami, Antonino Natalello, Pietro Gatti-Lafranconi, Marina Lotti, Silvia Maria Doglia,