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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.
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.
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 ...
Example of a Stiff diagram. A typical Stiff diagram is shown in the figure (right). By standard convention, Stiff diagrams are created by plotting the equivalent concentration of the cations to the left of the center axis and anions to the right. The points are connected to form the figure.
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 ...
Walsh Diagram of an HAH molecule. Walsh diagrams, often called angular coordinate diagrams or correlation diagrams, are representations of calculated orbital binding energies of a molecule versus a distortion coordinate (bond angles), used for making quick predictions about the geometries of small molecules.
Craig plot showing values of Hansch pi and Hammett sigma constants for 26 common organic substituents. 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