Vibrational spectroscopy of semiheavy water (HDO) as a probe of solute hydration

Śmiechowski, Maciej; Stangret, Janusz

doi:10.1351/pac-con-09-10-14

Cited by 45 publications

(37 citation statements)

References 90 publications

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“…An assumption was made that the water in solution can be divided into two additive contributions: the “bulk” water (identical to pure water) and “affected” water, the qualities of which have been affected by interactions with the solute. The method was described in detail in Stangret ( 1988 ), Stangret and Gampe ( 1999 ) and Śmiechowski and Stangret ( 2010 ), and some of the most basic information are included in section S1 (ESM).…”

Section: Methodsmentioning

confidence: 99%

Taurine as a water structure breaker and protein stabilizer

et al. 2017

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The enhancing effect on the water structure has been confirmed for most of the osmolytes exhibiting both stabilizing and destabilizing properties in regard to proteins. The presented work concerns osmolytes, which should be classified as “structure breaking” solutes: taurine and N,N,N-trimethyltaurine (TMT). Here, we combine FTIR spectroscopy, DSC calorimetry and DFT calculations to gain an insight into the interactions between osmolytes and two proteins: lysozyme and ubiquitin. Despite high structural similarity, both osmolytes exert different influence on protein stability: taurine is a stabilizer, TMT is a denaturant. We show also that taurine amino group interacts directly with the side chains of proteins, whereas TMT does not interact with proteins at all. Although two solutes weaken on average the structure of the surrounding water, their hydration spheres are different. Taurine is surrounded by two populations of water molecules: bonded with weak H-bonds around sulfonate group, and strongly bonded around amino group. The strong hydrogen-bonded network of water molecules around the amino group of taurine further improves properties of enhanced protein hydration sphere and stabilizes the native protein form. Direct interactions of this group with surface side chains provide a proper orientation of taurine and prevents the group from negative influence. The weakened hydration sphere of TMT breaks up the hydrogen-bonded network of water around the protein and destabilizes it. However, TMT at low concentration stabilize both proteins to a small extent. This effect can be attributed to an actual osmophobic effect which is overcome if the concentration increases.Electronic supplementary materialThe online version of this article (doi:10.1007/s00726-017-2499-x) contains supplementary material, which is available to authorized users.

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Section: Methodsmentioning

confidence: 99%

Taurine as a water structure breaker and protein stabilizer

et al. 2017

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“…The difference spectra method was used to extract the solute-affected HDO spectrum, extrapolated to the very diluted solution limit on the basis of spectra series, which were measured for different molalities of aqueous solutions. The method was described in detail in References [54][55][56]. This method assumes that water in a solution can be divided into two types: the "bulk" water (i.e., water exhibiting the properties of pure water) and "affected" water (i.e., water changed by interactions with the solute).…”

Section: Spectral Data Analysismentioning

confidence: 99%

Hydration of Simple Model Peptides in Aqueous Osmolyte Solutions

Panuszko

Pieloszczyk

Kuffel

et al. 2021

IJMS

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The biology and chemistry of proteins and peptides are inextricably linked with water as the solvent. The reason for the high stability of some proteins or uncontrolled aggregation of others may be hidden in the properties of their hydration water. In this study, we investigated the effect of stabilizing osmolyte–TMAO (trimethylamine N-oxide) and destabilizing osmolyte–urea on hydration shells of two short peptides, NAGMA (N-acetyl-glycine-methylamide) and diglycine, by means of FTIR spectroscopy and molecular dynamics simulations. We isolated the spectroscopic share of water molecules that are simultaneously under the influence of peptide and osmolyte and determined the structural and energetic properties of these water molecules. Our experimental and computational results revealed that the changes in the structure of water around peptides, caused by the presence of stabilizing or destabilizing osmolyte, are significantly different for both NAGMA and diglycine. The main factor determining the influence of osmolytes on peptides is the structural-energetic similarity of their hydration spheres. We showed that the chosen peptides can serve as models for various fragments of the protein surface: NAGMA for the protein backbone and diglycine for the protein surface with polar side chains.

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“…It has already provided a substantial library of spectral data on ionic solutes, as reviewed previously in detail. 39 , 40 …”

Section: Methodsmentioning

confidence: 99%

Hydration of Oxometallate Ions in Aqueous Solution

Śmiechowski

Persson

2020

Inorg. Chem.

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The strength of hydrogen bonding to and structure of hydrated oxometallate ions in aqueous solution have been studied by double difference infrared (DDIR) spectroscopy and large-angle X-ray scattering (LAXS), respectively. Anions are hydrated by accepting hydrogen bonds from the hydrating water molecules. The oxygen atom of the permanganate and perrhenate ions form weaker and longer hydrogen bonds to water than the hydrogen bonds in bulk water (i.e., they act as structure breakers), while the oxygen atoms of the chromate, dichromate, molybdate, tungstate, and hydrogenvanadate ions form hydrogen bonds stronger than those in bulk water (i.e., they act as structure makers). The oxometallate ions form one hydration shell distinguishable from bulk water as determined by DDIR spectroscopy and LAXS. The hydration of oxoanions results in X–O bond distances ca. 0.02 Å longer than those in unsolvated ions in the solid state not involved in strong bonding to counterions. The oxygens of oxoanions with a central atom from the second and third series in the periodic table and the hydrogenvanadate ion hydrogen bind three hydrating water molecules, while oxygens of oxoanions with a heavier central atom only form hydrogen bonds to two water molecules.

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Vibrational spectroscopy of semiheavy water (HDO) as a probe of solute hydration

Cited by 45 publications

References 90 publications

Taurine as a water structure breaker and protein stabilizer

Taurine as a water structure breaker and protein stabilizer

Hydration of Simple Model Peptides in Aqueous Osmolyte Solutions

Hydration of Oxometallate Ions in Aqueous Solution

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