The microscopic mechanisms of the proteins folding/unfolding process studied by means of FTIR and NMR spectroscopies.

Mallamace D., Longo S., Fazio E., Corsaro C.

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V - Biofisica e fisica medica
Aula 32C-2 - Mercoledì 19 h 09:00 - 13:00
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We study the microscopic mechanisms that underlie the folding/unfolding process of proteins by means of FTIR and NMR spectroscopies. In particular, by following the thermal evolution of the Amide I and II vibrational modes of lysozyme residues from ambient temperature up to the irreversible unfolding temperature, we are able to describe and characterize the entire process. NMR experiments confirm the determinant role played by the hydrogen bond coupling between hydration water and protein hydrophilic groups. Furthermore, the observation of the infrared bands characteristic of alpha helices and beta sheets allows to gain insights into the corresponding aggregation state.

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