The role of the H-bond network in the creation of the life-giving properties of water

Fisenko, Anatoliy I.; Malomuzh, N. P.

doi:10.1016/j.chemphys.2007.08.013

Cited by 23 publications

(18 citation statements)

References 18 publications

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“…One can see that, to the left from the singular point, the clustering degree of alcohol molecules monotonically increases with both the concentration and temperature. This fact absolutely correlates with the conclusions of works [35][36][37], in which it was shown that liquid water demonstrates quasicrystalline properties up to the characteristic temperature ≈ (42 ± 3) ∘ C. Near this temperature (at = 40 ∘ C), a ( , ) approaches unity when starting from low ethanol concentrations (see Fig. 1).…”

Section: Clustering Degree In Aqueous Ethanol Solutionssupporting

confidence: 89%

Qualitative Analysis of Clustering in Aqueous Alcohol Solutions. II

Chechko¹,

Gotsulskiy

Diieva

2019

Ukr. J. Phys.

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Specific features of the clustering in aqueous solutions of monoatomic alcohols have been discussed. Main attention is focused on details of the clustering in water-ethanol solutions. The clustering degree is supposed to depend on the nteraction between ethanol and water molecules, as well as on the ordering degree of the H-bond network in water, which changes with the temperature and concentration of the alcohol. The elementary cluster volume is assumed to be smaller than the sum of the molecular volumes of components that form this cluster. The clustering degree in aqueous solutions of methanol and ethanol and its concentration and temperature dependences are determined.

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Section: Clustering Degree In Aqueous Ethanol Solutionssupporting

confidence: 89%

Qualitative Analysis of Clustering in Aqueous Alcohol Solutions. II

Chechko¹,

Gotsulskiy

Diieva

2019

Ukr. J. Phys.

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“…A transition from the crystal-like to argon-like thermal motion can be qualified as a dynamic phase transition in water [16,17]. This conclusion is very important because of the problems of protein denaturation in inner cell water [17].…”

Section: Water Structure According To the Data Of Dipole Relaxation Amentioning

confidence: 99%

Cluster structure of water in accordance with the data on dielectric permittivity and heat capacity

Malomuzh

Makhlaichuk

et al. 2013

J Struct Chem

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In the work the character of water clusterization in the whole existence domain of its liquid state is discussed: from supercooled states to the critical point. Conclusions about the cluster composition of liquid water are drawn based on the analysis: 1) of the features of dielectric relaxation; 2) character of the temperature dependence of its static dielectric permittivity, and 3) the value and temperature dependence of different contributions to the heat capacity of the system. It is shown that near the water crystallization point tetramers prevail in its structure, with an increase in the temperature trimers start to play the main role, and near the critical point of water dimers become the major associates. At temperatures near the water crystallization point the obtained results well agree with the data on emission and absorption X-ray spectroscopy.

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“…In particular, it was shown that, at the temperature ≈ 42 ∘ C, the crystal-like character of the thermal motion of water molecules transforms into an argon-like one, which corresponds to the absence of clustering. This temperature is known to be the upper limit for human life or, in terms of the existence of some proteins, the temperature of their denaturation [8][9][10]. In effect, this means that a long evolution of primitive proteins in the ocean has led to the adjustment of their most important properties to those of water, in particular, to the temperature at which the character of thermal motion of water molecules changes.…”

Section: Introductionmentioning

confidence: 99%

Crucial Role of Water in the Formation of Basic Properties of Living Matter

Булавин¹,

Gotsulskyi²,

Malomuzh³

et al. 2020

Ukr. J. Phys.

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A relation between the water properties and the behavior of aqueous solutions of albumin, the main protein component of human blood plasma, has been analyzed. The dependence of the pH index of acid-base balance in aqueous albumin solutions on the albumin concentration is experimentally studied. It is shown that the temperature dependences of pH in biological solutions are determined by the properties of water, and the concentration ones by the concentration of a protein component. It is albumin that makes the main contribution to the pHs of blood and blood plasma, and it should be considered as a factor that maintains the equilibrium pH value. It is shown that the most characteristic changes in the concentration dependences of the density and shear viscosity of human plasma occur at a protein concentration corresponding to the percolation threshold. A characteristic dimerization of albumin macromolecules is assumed to take place at the percolation threshold, which corresponds to the superposition on one another of heart-shaped medallions representing the spatial forms of albumin. The dependences of the effective radii of polyvinyl alcohol and albumin macromolecules on the solution temperature and concentration are demonstrated to be an indicator that water plays a decisive role in the formation of basic properties of biosolutions. In particular, it is responsible for the presence of an upper temperature limit of 42 ∘C for the existence of living matter. The universal nature of the water influence manifests itself in that the water properties affect the behavior of both the classic PVA polymer and protein biomolecules.

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The role of the H-bond network in the creation of the life-giving properties of water

Cited by 23 publications

References 18 publications

Qualitative Analysis of Clustering in Aqueous Alcohol Solutions. II

Qualitative Analysis of Clustering in Aqueous Alcohol Solutions. II

Cluster structure of water in accordance with the data on dielectric permittivity and heat capacity

Crucial Role of Water in the Formation of Basic Properties of Living Matter

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