Dynamical properties of myoglobin in an ultraviscous water-glycerol solvent investigated with elastic neutron scattering and FTIR spectroscopy

Librizzi, Fabio; Caliò, Antonino; Cupane, Antonio

doi:10.1016/j.molliq.2018.07.050

Journal of Molecular Liquids

2018

DOI: 10.1016/j.molliq.2018.07.050

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Dynamical properties of myoglobin in an ultraviscous water-glycerol solvent investigated with elastic neutron scattering and FTIR spectroscopy

Fabio Librizzi

Antonino Caliò

Antonio Cupane

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2019

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Cited by 2 publications

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“…The protein dynamical transition (PDT) and its correlation with the external medium have been investigated by Librizzi and coworkers using temperature dependent elastic neutron scattering (ENS) and IR absorption. Experimental data on myoglobin in water-glycerol, indi-cates the occurrence of coupling between the dynamics of protein back-bone and the fluctuations of amino acid side chains, both processes are thought to be mediated by the solvent [7].…”

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confidence: 99%

Editorial of virtual special issue Frontiers in Water Biophysics 2017

Paolantoni

Cesàro

Comez

et al. 2019

Journal of Molecular Liquids

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confidence: 99%

Editorial of virtual special issue Frontiers in Water Biophysics 2017

Paolantoni

Cesàro

Comez

et al. 2019

Journal of Molecular Liquids

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Multiple Glass-Transitions of Globular Protein BSA Aqueous Solutions Depending on the Hydration Degree

Watanabe

Kawai

Nagoe

et al. 2019

Bulletin of the Chemical Society of Japan

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Glass-transition behavior of hydrated bovine serum albumin (BSA) aqueous solutions depending on hydration degree within 0.05 and 0.43 h (water-g/protein-g) was investigated according to the measurement of an enthalpy-relaxation rate deduced from the temperature drift observed by adiabatic calorimetry. The results showed that an increase in hydration degree enlarged the temperature range in which the enthalpy-relaxation effects emerged. The BSA sample in hydration degree around 0.05 h showed one Tg peak, and further hydration to 0.24 h led to up to three distinguishable Tg, and finally BSA solution of 0.43 h showed cold crystallization due to the portion of water molecules included. The multiplicity of the Tg in the well-hydrated BSA is explained as follows: At sufficiently low temperatures, ∼50 K, the hydrated BSA molecule and the contained water molecules are completely frozen. Then, heating induces mobility of some of the water molecules initially, and further causes the sequential unfreezing of the polar side chains of BSA molecules, coupling with the directly hydrating water molecules, and, in turn, of the main chains of the BSA molecule. This interpretation may integrate the unique insights of glass transition behavior of hydrated proteins into a consensus.

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Dynamical properties of myoglobin in an ultraviscous water-glycerol solvent investigated with elastic neutron scattering and FTIR spectroscopy

Cited by 2 publications

References 59 publications

Editorial of virtual special issue Frontiers in Water Biophysics 2017

Editorial of virtual special issue Frontiers in Water Biophysics 2017

Multiple Glass-Transitions of Globular Protein BSA Aqueous Solutions Depending on the Hydration Degree

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