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Hydrophobicity scales are values that define the relative hydrophobicity or hydrophilicity of amino acid residues. The more positive the value, the more hydrophobic are the amino acids located in that region of the protein. These scales are commonly used to predict the transmembrane alpha-helices of membrane proteins.
Hence the hydrophobicity of a compound (as measured by its distribution coefficient) is a major determinant of how drug-like it is. More specifically, for a drug to be orally absorbed, it normally must first pass through lipid bilayers in the intestinal epithelium (a process known as transcellular transport). For efficient transport, the drug ...
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 .
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.
In biochemistry, the hydrophobic effect can be used to separate mixtures of proteins based on their hydrophobicity. Column chromatography with a hydrophobic stationary phase such as phenyl-sepharose will cause more hydrophobic proteins to travel more slowly, while less hydrophobic ones elute from the column sooner. To achieve better separation ...
The n-octanol-water partition coefficient, K ow is a partition coefficient for the two-phase system consisting of n-octanol and water. [1] K ow is also frequently referred to by the symbol P, especially in the English literature.
Some of the major driving forces behind protein adsorption include: surface energy, intermolecular forces, hydrophobicity, and ionic or electrostatic interaction. By knowing how these factors affect protein adsorption, they can then be manipulated by machining, alloying, and other engineering techniques to select for the most optimal ...
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 ...