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• W56224680 abstract "Recently, it has been recognized that protein's folding and unfolding mechanisms exhibit a wide range of common features with the glass transition observed in supercooled organic and inorganic liquids. Such similarities range from pure thermodynamic aspects such an anomalous ΔCp and a substantial entropy decrease ΔS<0, to strictly kinetic aspects as the existence of an excess of vibrational modes at low frequencies (bosonic peak) revealed by Raman and neutron scattering experiments. In this work, we discuss both the experimental and theoretical facts that might enable an extrapolation of the Adam‐Gibbs scheme for the standard glass transition to describe the relaxation time τ as function of temperature T in biological macromolecules' unfolding." @default.
• W56224680 created "2016-06-24" @default.
• W56224680 creator A5068764666 @default.
• W56224680 creator A5079855410 @default.
• W56224680 date "2008-01-01" @default.
• W56224680 modified "2023-10-16" @default.
• W56224680 title "Protein's unfolding and the glass transition: a common thermodynamic signature." @default.
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• W56224680 doi "https://doi.org/10.1063/1.2891407" @default.
• W56224680 hasPublicationYear "2008" @default.
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