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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.
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 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. [1] [2]
For efficient transport, the drug must be hydrophobic enough to partition into the lipid bilayer, but not so hydrophobic, that once it is in the bilayer, it will not partition out again. [ 29 ] [ 30 ] Likewise, hydrophobicity plays a major role in determining where drugs are distributed within the body after absorption and, as a consequence, in ...
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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]
For dogs and cats, a 9 point body condition score (BCS) system is used to identify whether they are above their ideal weight status. [5] Scores 1-3 indicate 'too thin', 4 and 5 are 'ideal', 6 is 'above ideal', 7 is 'overweight' and 8 and 9 are 'obese'.
The cysteine residues participate in establishing disulfide linkages within and among mucin monomers. A large central region ("PTS domain") formed of multiple tandem repeats of 10 to 80 residue sequences in which up to half of the amino acids are serine or threonine. This area becomes saturated with hundreds of O-linked oligosaccharides.