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The absolute values and relative rankings of hydrophobicity determined by chromatographic methods can be affected by a number of parameters. These parameters include the silica surface area and pore diameter, the choice and pH of aqueous buffer, temperature and the bonding density of stationary phase chains.
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 ...
The constants listed here are known values of physical constants expressed in SI units; that is, physical quantities that are generally believed to be universal in nature and thus are independent of the unit system in which they are measured. Many of these are redundant, in the sense that they obey a known relationship with other physical ...
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.
[10]: 275ff When one of the solvents is water and the other is a non-polar solvent, then the log P value is a measure of lipophilicity or hydrophobicity. [ 10 ] : 275ff [ 11 ] : 6 The defined precedent is for the lipophilic and hydrophilic phase types to always be in the numerator and denominator respectively; for example, in a biphasic system ...
The Hopp–Woods hydrophilicity scale of amino acids is a method of ranking the amino acids in a protein according to their water solubility in order to search for surface locations on proteins, and especially those locations that tend to form strong interactions with other macromolecules such as proteins, DNA, and RNA.
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 .
Note that the especially high molar values, as for paraffin, gasoline, water and ammonia, result from calculating specific heats in terms of moles of molecules. If specific heat is expressed per mole of atoms for these substances, none of the constant-volume values exceed, to any large extent, the theoretical Dulong–Petit limit of 25 J⋅mol ...