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Related Concept Videos

Hydration of Cement01:24

Hydration of Cement

953
Hydration of cement is a chemical reaction between cement particles and water. This process occurs primarily through two mechanisms: through-solution and topochemical. In the through-solution process, anhydrous compounds dissolve into their constituents, hydrates form in the solution, and then precipitate from the supersaturated solution. The topochemical process involves solid-state reactions at the cement particle surface. The through-solution process dominates the topochemical process at the...
953
Aqueous Solutions and Heats of Hydration02:42

Aqueous Solutions and Heats of Hydration

18.0K
Water and other polar molecules are attracted to ions. The electrostatic attraction between an ion and a molecule with a dipole is called an ion-dipole attraction. These attractions play an important role in the dissolution of ionic compounds in water.
When ionic compounds dissolve in water, the ions in the solid separate and disperse uniformly throughout the solution because water molecules surround and solvate the ions, reducing the strong electrostatic forces between them. This process...
18.0K
Range00:59

Range

14.3K
The range is one of the measures of variation. It can be defined as the difference between a dataset's highest and lowest values. For example, in the study of seven 16-ounce soda cans, the filled volume of soda was measured, thus producing the following amount (in ounces) of soda:
15.9; 16.1; 15.2; 14.8; 15.8; 15.9; 16.0; 15.5
Measurements of the amount of soda in a 16-ounce can vary since different subjects record these measurements or since the exact amount - 16 ounces of liquid, was not...
14.3K
Strength and Heat of Hydration01:29

Strength and Heat of Hydration

707
The hydration of cement is an exothermic reaction in which heat is generated as cement hydrates. This heat of hydration is critical to cement's strength development. The rate at which this heat is generated affects the temperature rise, with a majority of the heat being released early in the hydration process, half within the first three days, and about 75% within the first week.
The heat of hydration for each cement compound is significant; for instance, tricalcium aluminate (C3A) and...
707
¹H NMR: Long-Range Coupling01:27

¹H NMR: Long-Range Coupling

2.7K
The coupling interactions of nuclei across four or more bonds are usually weak, with J values less than 1 Hz. While these are usually not observed in spectra, the presence of multiple bonds along the coupling pathway can result in observable long-range coupling.
In alkenes, spin information is communicated via σ–π overlap, as seen in allylic (four-bond) and homoallylic (five-bond) couplings. These coupling interactions are stronger when the σ bond is parallel to the alkene...
2.7K
Acid-Catalyzed Hydration of Alkenes02:45

Acid-Catalyzed Hydration of Alkenes

17.3K
Alkenes react with water in the presence of an acid to form an alcohol. In the absence of acid, hydration of alkenes does not occur at a significant rate, and the acid is not consumed in the reaction. Therefore, alkene hydration is an acid-catalyzed reaction.
17.3K

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Updated: Feb 9, 2026

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
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The spatial range of protein hydration.

Filip Persson1, Pär Söderhjelm1, Bertil Halle1

  • 1Division of Biophysical Chemistry, Department of Chemistry, Lund University, P.O. Box 124, SE-22100 Lund, Sweden.

The Journal of Chemical Physics
|June 10, 2018
PubMed
Summary

Protein interactions with water are short-ranged, with solvent properties returning to bulk values within one hydration shell. This finding stems from water

Area of Science:

  • Biophysics
  • Physical Chemistry
  • Computational Biology

Background:

  • Proteins interact with surrounding water, altering its physical properties.
  • The spatial extent of protein-induced solvent perturbation remains debated.
  • A clear definition of perturbation range is lacking in current literature.

Purpose of the Study:

  • To define and analyze the decay length of protein-induced solvent perturbations.
  • To investigate the structural and dynamic properties of the hydrogen-bonded solvent network around proteins.
  • To clarify the range of solvent structural and dynamic modifications by proteins.

Main Methods:

  • Molecular dynamics simulations of four small globular proteins.
  • Analysis of structural and dynamic properties of the water solvent network.

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  • Calculation of exponential decay lengths for solvent properties.

    • Main Results:

    • Solvent perturbation by proteins is unequivocally short-ranged.
    • All investigated solvent properties exhibit decay lengths within one hydration shell.
    • Bulk water's high energy density resists structural perturbations.
    • Protein electric fields induce only weak, linear dielectric responses in water dipoles.
    • Nonpolar protein surface hydration resembles that of small nonpolar solutes.
    • Water-water hydrogen bonds near nonpolar surfaces are similar to bulk water.

    Conclusions:

    • Protein-induced solvent perturbations are limited to the immediate hydration shell.
    • The protein electric field's effect on water is a linear dielectric response, not a structural perturbation.
    • Protein surface topography minimizes hydrophobic hydration free energy, reducing aggregation propensity.