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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.
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.
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.
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.
HLB scale showing classification of surfactant function. The hydrophilic–lipophilic balance (HLB) of a surfactant is a measure of its degree of hydrophilicity or lipophilicity, determined by calculating percentages of molecular weights for the hydrophilic and lipophilic portions of the surfactant molecule, as described by Griffin in 1949 [1] [2] and 1954. [3]
In biochemistry, a Ramachandran plot (also known as a Rama plot, a Ramachandran diagram or a [φ,ψ] plot), originally developed in 1963 by G. N. Ramachandran, C. Ramakrishnan, and V. Sasisekharan, [1] is a way to visualize energetically allowed regions for backbone dihedral angles ( also called as torsional angles , phi and psi angles ) ψ ...
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 ...
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.
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