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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.
About a decade ago, another hydrophilicity scale was published, this scale used normal phase liquid chromatography and showed the retention of 121 peptides on an amide-80 column. [28] The absolute values and relative rankings of hydrophobicity determined by chromatographic methods can be affected by a number of parameters.
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.
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).
An approximate rule of thumb for hydrophilicity of organic compounds is that solubility of a molecule in water is more than 1 mass % if there is at least one neutral hydrophile group per 5 carbons, or at least one electrically charged hydrophile group per 7 carbons. [4] Hydrophilic substances (ex: salts) can seem to attract water out of the air.
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 Stiff diagram, or Stiff pattern, is a graphical representation of chemical analyses, first developed by H.A. Stiff in 1951.It is widely used by hydrogeologists and geochemists to display the major ion composition of a water sample.
This modification is usually made to solid materials, but it is possible to find examples of the modification to the surface of specific liquids. The modification can be done by different methods with a view to altering a wide range of characteristics of the surface, such as: roughness, [ 2 ] hydrophilicity, [ 3 ] surface charge, [ 4 ] surface ...