Influence of temperature on hydration-shell microstructure of chlorine and bromine anions in aqueous solution

Donets, Alexey V.; Chizhik, Vladimir I.

doi:10.1007/s11224-011-9767-2

Cited by 8 publications

(10 citation statements)

References 13 publications

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“…As it could be seen from values of τ b and K d , the chlorine ions seem to be in tighter contact with the protein than sodium ones. This fact is also consistent with the previously observed pattern [48].…”

Section: Concentration Dependences Of R 1 and R 2 For 1 H 2 H 23 Nasupporting

confidence: 94%

“…For the 0.6 mM concentration of RRM2, the R 2 rates for 23 Na and 35 Cl increase by 12% and 60%, respectively. Such a strong protein effect on the relaxation of ions nuclei was observed earlier [26,27,30,48]. It could be seen that in the buffer R 1 = R 2 for both ions but at higher protein concentrations, the difference between R 1 and R 2 increases.…”

Section: Concentration Dependences Of R 1 and R 2 For 1 H 2 H 23 Nasupporting

confidence: 71%

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NMR Relaxation of Nuclei of Buffer as a Probe for Monitoring Protein Solutions Including Aggregation Processes

et al. 2020

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Characterization of protein solutions is of great importance for biophysical research, pharmaceutical industry, and medicine. Particularly, the monitoring of the protein aggregation is crucial at all stages of biotechnological production and in the diagnosis of dangerous diseases. The present work is focused on a study of prospects and possibilities of NMR relaxation of solvent nuclei for monitoring the state of proteins in solutions. The spin-lattice and spin-spin relaxation rates (R 1 and R 2) of solvent nuclei were measured in the solutions of a small globular protein, RRM2 domain of TDP-43 protein. The solvent was either H 2 O-or D 2 O-based buffer with pH 6.5 and contained 20 mM sodium phosphate and 150 mM NaCl. The relaxation rates of the solvent 1 H, 2 H, 23 Na, and 35 Cl nuclei in solutions of soluble and aggregated RRM2 domain of TDP-43 protein were studied. The aggregation was induced by mild oxidative stress, using treatment by hydrogen peroxide. It was found that aggregation of protein could be detected using NMR relaxation of 1 H nuclei. The observed CPMG dispersion for R 2 rates confirms the millisecond timescale for the hydrogen exchange between water and protein sites. The correlation times and binding constants for sodium and chlorine ions were estimated using concentration dependences for relaxation rates (23 Na, 35 Cl). The relaxation rates of solvent nuclei are sensitive to the presence of protein in solution even at low protein concentrations, and the relaxation rates of different nuclei reflect various aspects of the state of the protein.

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Section: Concentration Dependences Of R 1 and R 2 For 1 H 2 H 23 Nasupporting

confidence: 94%

Section: Concentration Dependences Of R 1 and R 2 For 1 H 2 H 23 Nasupporting

confidence: 71%

NMR Relaxation of Nuclei of Buffer as a Probe for Monitoring Protein Solutions Including Aggregation Processes

et al. 2020

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“…The study by Donets and Chizhik [131] offers a possible explanation for the thermoregulation of warm-blooded animals. The change of the microstructure of the hydration shell of Cl -and Br -anions within the temperature range of 30-35°C has been shown.…”

Section: Issuementioning

confidence: 99%

Interplay of thermochemistry and Structural Chemistry, the Journal (volume 22, 2011, issues 1–3) and the discipline

Ponikvar‐Svet

Liebman

2011

Struct Chem

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“…В работах [8,9], посвященных влиянию анионов на ферментативный гидролиз АТФ, предложена гипотеза о влиянии анионов на неферментативный гидролиз АТФ с учетом непосредственного воздействия воды на реакцию гидролиза. В гипотезе обосновано возможное влияние обнаруженного эффекта изменения свойств гидратации анионов Cl − при изменении температуры на активность реакций ферментативного и неферментативного гидролиза АТФ [10,11]. Анион хлора -это один из основных анионов, находящихся в крови, в клеточной и межклеточной жидкости.…”

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“…Эффект изменения свойств гидратации анионов хлора. Однако, как было сказано в работе [11], у некоторых анионов, например, у аниона хлора, был обнаружен температурный эффект изменения координации, т.е. микроструктуры гидратных оболочек или изменения свойств гидратации данного аниона.…”

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TEMPERATURE EFFECT OF CHANGES IN THE HYDRATION PROPERTIES OF THE Cl- ANION IN HUMAN BLOOD

2020

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The work with the biological objects has been carried out on the basis of a previously developed methodology for the study of the hydration properties of various molecular groups in solutions containing organic components. The nuclear magnetic resonance (NMR) method has become the main experimental method, with the help of which it has become possible to detect and theoretically describe the temperature effect of changing the hydration properties of certain anions in water-salt and multicomponent solutions. This effect has also been recorded for the anions of chlorine, one of the most common chemical elements in the bodies of the living tissue. This work is a continuation of a series of works on the study of the possible influence of this effect on the thermoregulation of living tissue. This work is carried out at the confluence of physics, chemistry and biology, taking into account the knowledge accumulated in the world on the physical and chemical description of the systems under study to obtain an explanation of a biologically significant result. For the first time, such a study was carried out with biological objects characteristic of the human body - with blood and saliva. This effect should work throughout the whole body, given the presence of blood in all its structures. In the study of saliva which has been carried out, this effect was found as well. The results of the work expand and clarify the previously proposed hypothesis of thermoregulation of warm-blooded living tissue. The proposed feedback in the energy processes control system should work with different biological solutions characteristic of living objects. The work implements an approach notable for its logical simplicity, but at the same time this approach allows to connect the latest possibilities of modern science in the field of interdisciplinary research.

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Influence of temperature on hydration-shell microstructure of chlorine and bromine anions in aqueous solution

Cited by 8 publications

References 13 publications

NMR Relaxation of Nuclei of Buffer as a Probe for Monitoring Protein Solutions Including Aggregation Processes

NMR Relaxation of Nuclei of Buffer as a Probe for Monitoring Protein Solutions Including Aggregation Processes

Interplay of thermochemistry and Structural Chemistry, the Journal (volume 22, 2011, issues 1–3) and the discipline

TEMPERATURE EFFECT OF CHANGES IN THE HYDRATION PROPERTIES OF THE Cl- ANION IN HUMAN BLOOD

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