Dielectric Relaxation of Hydration Water in Native Collagen Fibrils

© 2017 American Chemical Society. The dielectric relaxation of hydrated collagen powders was studied over a wide temperature and frequency range. We revealed two mechanisms of dielectric relaxation in hydration water that are driven by the migration of ionic and orientation defects. At high water fractions in powders (h > 0.2), the hydration shell around the collagen triple helixes presents a spatial H-bonded network consisting of structural water bridges and cleft water channels. These two water phases provide the long-range paths for proton hopping and orientation defect migration. At low water fractions (h < 0.2) and in the hydrated collagen samples after the dehydrothermal treatment, the hydration shell presents localized individual water compartments not connected to one another. In these cases, the relaxation mechanism due to proton hopping either disappears or becomes inhibited by the orientation defect migration

Dielectric Relaxation of Hydration Water in Native Collagen Fibrils

© 2017 American Chemical Society. The dielectric relaxation of hydrated collagen powders was studied over a wide temperature and frequency range. We revealed two mechanisms of dielectric relaxation in hydration water that are driven by the migration of ionic and orientation defects. At high water fractions in powders (h > 0.2), the hydration shell around the collagen triple helixes presents a spatial H-bonded network consisting of structural water bridges and cleft water channels. These two water phases provide the long-range paths for proton hopping and orientation defect migration. At low water fractions (h < 0.2) and in the hydrated collagen samples after the dehydrothermal treatment, the hydration shell presents localized individual water compartments not connected to one another. In these cases, the relaxation mechanism due to proton hopping either disappears or becomes inhibited by the orientation defect migration

The role of the confined water in the dynamic crossover of hydrated lysozyme powders

© the Owner Societies 2016.Water is of fundamental importance for life since it plays a critical role in biological systems. An organism can only function if its macromolecules and other bioactive molecules are hydrated. However, currently there is a gap in the understanding of how protein interfaces affect water's structure and properties. This work presents combined dielectric and calorimetric measurements of hydrated lysozyme powders with different levels of hydration in a broad temperature interval. We chose lysozyme as a test sample since this globular protein has a well-defined pore with an active hydrophilic center inside. Based on the dielectric and calorimetric tests it was shown that a water quasi-solution, which contains the protein residues, has a glass transition temperature at around 155 ± 3 K. The water confined in the pore of the active center of the lysozyme has its melting temperature at around 186 ± 3 K. Melting of confined water is believed to liberate the internal motions of protein macromolecules

Confined water dynamics in a hydrated photosynthetic pigment-protein complex

© This journal is the Owner Societies. Water is of fundamental importance for life. It plays a critical role in all biological systems. In p hycocyanin, a pigment-protein complex, the hydration level influences its absorption spectrum. However, there is currently a gap in the understanding of how protein interfaces affect water's structure and properties. This work presents combined dielectric and calorimetric measurements of hydrated phycocyanin with different levels of hydration in a broad temperature interval. Based on the dielectric and calorimetric tests, it was shown that two types of water exist in the phycocyanin hydration shell. One is confined water localized inside the phycocyanin ring and the second is the water that is embedded in the protein structure and participates in the protein solvation. The water confined in the phycocyanin ring melts at the temperature 195 ± 3 K and plays a role in the solvation at higher temperatures. Moreover, the dynamics of all types of water was found to be effected by the presence of the ionic buffer

Dielectric Relaxation of Hydration Water in Native Collagen Fibrils

© 2017 American Chemical Society. The dielectric relaxation of hydrated collagen powders was studied over a wide temperature and frequency range. We revealed two mechanisms of dielectric relaxation in hydration water that are driven by the migration of ionic and orientation defects. At high water fractions in powders (h > 0.2), the hydration shell around the collagen triple helixes presents a spatial H-bonded network consisting of structural water bridges and cleft water channels. These two water phases provide the long-range paths for proton hopping and orientation defect migration. At low water fractions (h < 0.2) and in the hydrated collagen samples after the dehydrothermal treatment, the hydration shell presents localized individual water compartments not connected to one another. In these cases, the relaxation mechanism due to proton hopping either disappears or becomes inhibited by the orientation defect migration

The role of the confined water in the dynamic crossover of hydrated lysozyme powders

© the Owner Societies 2016.Water is of fundamental importance for life since it plays a critical role in biological systems. An organism can only function if its macromolecules and other bioactive molecules are hydrated. However, currently there is a gap in the understanding of how protein interfaces affect water's structure and properties. This work presents combined dielectric and calorimetric measurements of hydrated lysozyme powders with different levels of hydration in a broad temperature interval. We chose lysozyme as a test sample since this globular protein has a well-defined pore with an active hydrophilic center inside. Based on the dielectric and calorimetric tests it was shown that a water quasi-solution, which contains the protein residues, has a glass transition temperature at around 155 ± 3 K. The water confined in the pore of the active center of the lysozyme has its melting temperature at around 186 ± 3 K. Melting of confined water is believed to liberate the internal motions of protein macromolecules

The role of the confined water in the dynamic crossover of hydrated lysozyme powders

© the Owner Societies 2016.Water is of fundamental importance for life since it plays a critical role in biological systems. An organism can only function if its macromolecules and other bioactive molecules are hydrated. However, currently there is a gap in the understanding of how protein interfaces affect water's structure and properties. This work presents combined dielectric and calorimetric measurements of hydrated lysozyme powders with different levels of hydration in a broad temperature interval. We chose lysozyme as a test sample since this globular protein has a well-defined pore with an active hydrophilic center inside. Based on the dielectric and calorimetric tests it was shown that a water quasi-solution, which contains the protein residues, has a glass transition temperature at around 155 ± 3 K. The water confined in the pore of the active center of the lysozyme has its melting temperature at around 186 ± 3 K. Melting of confined water is believed to liberate the internal motions of protein macromolecules

Dielectric Relaxation of Hydration Water in Native Collagen Fibrils

© 2017 American Chemical Society. The dielectric relaxation of hydrated collagen powders was studied over a wide temperature and frequency range. We revealed two mechanisms of dielectric relaxation in hydration water that are driven by the migration of ionic and orientation defects. At high water fractions in powders (h > 0.2), the hydration shell around the collagen triple helixes presents a spatial H-bonded network consisting of structural water bridges and cleft water channels. These two water phases provide the long-range paths for proton hopping and orientation defect migration. At low water fractions (h < 0.2) and in the hydrated collagen samples after the dehydrothermal treatment, the hydration shell presents localized individual water compartments not connected to one another. In these cases, the relaxation mechanism due to proton hopping either disappears or becomes inhibited by the orientation defect migration

The role of the confined water in the dynamic crossover of hydrated lysozyme powders

© the Owner Societies 2016.Water is of fundamental importance for life since it plays a critical role in biological systems. An organism can only function if its macromolecules and other bioactive molecules are hydrated. However, currently there is a gap in the understanding of how protein interfaces affect water's structure and properties. This work presents combined dielectric and calorimetric measurements of hydrated lysozyme powders with different levels of hydration in a broad temperature interval. We chose lysozyme as a test sample since this globular protein has a well-defined pore with an active hydrophilic center inside. Based on the dielectric and calorimetric tests it was shown that a water quasi-solution, which contains the protein residues, has a glass transition temperature at around 155 ± 3 K. The water confined in the pore of the active center of the lysozyme has its melting temperature at around 186 ± 3 K. Melting of confined water is believed to liberate the internal motions of protein macromolecules

Dielectric Relaxation of Hydration Water in Native Collagen Fibrils

© 2017 American Chemical Society. The dielectric relaxation of hydrated collagen powders was studied over a wide temperature and frequency range. We revealed two mechanisms of dielectric relaxation in hydration water that are driven by the migration of ionic and orientation defects. At high water fractions in powders (h > 0.2), the hydration shell around the collagen triple helixes presents a spatial H-bonded network consisting of structural water bridges and cleft water channels. These two water phases provide the long-range paths for proton hopping and orientation defect migration. At low water fractions (h < 0.2) and in the hydrated collagen samples after the dehydrothermal treatment, the hydration shell presents localized individual water compartments not connected to one another. In these cases, the relaxation mechanism due to proton hopping either disappears or becomes inhibited by the orientation defect migration