The protein irreversible denaturation studied by means of the bending vibrational mode

Domenico Mallamace, Carmelo Corsaro, Cirino Vasi, Sebastiano Vasi, Giacomo Dugo and Francesco Mallamace

Physica A: Statistical Mechanics and its Applications, 2014, vol. 412, issue C, 39-44

Abstract: We study by means of the infrared bending vibrational mode the microscopic mechanisms that are at the base of protein irreversible denaturation. In particular, we follow the thermal evolution of the Amide I and II vibrational modes of lysozyme residuals from ambient temperature toward the temperature of irreversible unfolding. Our results indicate that the thermal changes of the coupling, by means of the hydrogen bond, between hydration water molecules and the different chemical groups of the protein are the main microscopic mechanisms underlying the unfolding process.

Keywords: Protein denaturation; Amide bending; Lysozyme; Infrared spectroscopy (search for similar items in EconPapers)
Date: 2014
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Persistent link: https://EconPapers.repec.org/RePEc:eee:phsmap:v:412:y:2014:i:c:p:39-44

DOI: 10.1016/j.physa.2014.06.007

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