Dynamics of hydrated proteins and bio-protectants: Caged dynamics, β-relaxation, and α-relaxation

Biochimica Et Biophysica Acta. General Subjects
K L NgaiAlessandro Paciaroni

Abstract

The properties of the three dynamic processes, α-relaxation, ν-relaxation, and caged dynamics in aqueous mixtures and hydrated proteins are analogous to corresponding processes found in van der Waals and polymeric glass-formers apart from minor differences. Collection of various experimental data enables us to characterize the structural α-relaxation of the protein coupled to hydration water (HW), the secondary or ν-relaxation of HW, and the caged HW process. From the T-dependence of the ν-relaxation time of hydrated myoglobin, lysozyme, and bovine serum albumin, we obtain Ton at which it enters the experimental time windows of Mössbauer and neutron scattering spectroscopies, coinciding with protein dynamical transition (PDT) temperature Td. However, for all systems considered, the α-relaxation time at Ton or Td is many orders of magnitude longer. The other step change of the mean-square-displacement (MSD) at Tg_alpha originates from the coupling of the nearly constant loss (NCL) of caged HW to density. The coupling of the NCL to density is further demonstrated by another step change at the secondary glass temperature Tg_beta in two bio-protectants, trehalose and sucrose. The structural α-relaxation plays no role in PDT. Since ...Continue Reading

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Citations

Sep 23, 2016·Biochimica Et Biophysica Acta. General Subjects·C Austen AngellFederica Migliardo
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Jun 4, 2019·The Journal of Chemical Physics·Kaito SasakiYuri Feldman
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Jul 3, 2020·The Journal of Chemical Physics·Kerstin KämpfMichael Vogel
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Dec 6, 2017·The Journal of Physical Chemistry. B·Daniel R MartinDmitry V Matyushov

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