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For example, in the case of dissolved xenon at room temperature a mobility restriction of 30% has been found. [17] In the case of larger nonpolar molecules, the reorientational and translational motion of the water molecules in the solvation shell may be restricted by a factor of two to four; thus, at 25 °C the reorientational correlation time ...
A table comparing four different scales for the hydrophobicity of an amino acid residue in a protein with the most hydrophobic amino acids on the top. A number of different hydrophobicity scales have been developed. [3] [1] [7] [8] [9] The Expasy Protscale website lists a total of 22 hydrophobicity scales. [10]
The Craig plot, named after Paul N. Craig, is a plot of two substituent parameters (e.g. Hansch-Fujita π constant and sigma constant) used in rational drug design. [1] Two most used forms of a Craig plot are plotting the sigma constants of the Hammett equation versus hydrophobicity; plotting the steric terms of the Taft equation against ...
Cloth, treated to be hydrophobic, shows a high contact angle. The theoretical description of contact angle arises from the consideration of a thermodynamic equilibrium between the three phases: the liquid phase (L), the solid phase (S), and the gas or vapor phase (G) (which could be a mixture of ambient atmosphere and an equilibrium concentration of the liquid vapor).
For example, the constant π may be defined as the ratio of the length of a circle's circumference to its diameter. The following list includes a decimal expansion and set containing each number, ordered by year of discovery. The column headings may be clicked to sort the table alphabetically, by decimal value, or by set.
In chemistry, hydrophobicity is the chemical property of a molecule (called a hydrophobe) that is seemingly repelled from a mass of water. [1] In contrast, hydrophiles are attracted to water. Hydrophobic molecules tend to be nonpolar and, thus, prefer other neutral molecules and nonpolar solvents .
A hydrophilicity plot is a quantitative analysis of the degree of hydrophobicity or hydrophilicity of amino acids of a protein. It is used to characterize or identify possible structure or domains of a protein. The plot has amino acid sequence of a protein on its x-axis, and degree of hydrophobicity and hydrophilicity on its y-axis.
For example, the blood/gas partition coefficient of a general anesthetic measures how easily the anesthetic passes from gas to blood. [5] Partition coefficients can also be defined when one of the phases is solid , for instance, when one phase is a molten metal and the second is a solid metal, [ 6 ] or when both phases are solids. [ 7 ]