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  2. Hydrophobicity scales - Wikipedia

    en.wikipedia.org/wiki/Hydrophobicity_scales

    The hydrophobic effect represents the tendency of water to exclude non-polar molecules. The effect originates from the disruption of highly dynamic hydrogen bonds between molecules of liquid water. Polar chemical groups, such as OH group in methanol do not cause the hydrophobic effect.

  3. Hydrophobic effect - Wikipedia

    en.wikipedia.org/wiki/Hydrophobic_effect

    The hydrophobic effect is the observed tendency of nonpolar substances to aggregate in an aqueous solution and to be excluded by water. [ 1 ] [ 2 ] The word hydrophobic literally means "water-fearing", and it describes the segregation of water and nonpolar substances, which maximizes the entropy of water and minimizes the area of contact ...

  4. Alanine - Wikipedia

    en.wikipedia.org/wiki/Alanine

    Alanine (symbol Ala or A), [4] or α-alanine, is an α-amino acid that is used in the biosynthesis of proteins. It contains an amine group and a carboxylic acid group, both attached to the central carbon atom which also carries a methyl group side chain. Consequently it is classified as a nonpolar, aliphatic α-amino acid.

  5. Hydrophilicity plot - Wikipedia

    en.wikipedia.org/wiki/Hydrophilicity_plot

    Analyzing the shape of the plot gives information about partial structure of the protein. For instance, if a stretch of about 20 amino acids shows positive for hydrophobicity, these amino acids may be part of alpha-helix spanning across a lipid bilayer, which is composed of hydrophobic fatty acids. On the converse, amino acids with high ...

  6. Hydrophilic-lipophilic balance - Wikipedia

    en.wikipedia.org/wiki/Hydrophilic-lipophilic_balance

    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]

  7. Conservative replacement - Wikipedia

    en.wikipedia.org/wiki/Conservative_replacement

    A conservative replacement (also called a conservative mutation or a conservative substitution or a homologous replacement) is an amino acid replacement in a protein that changes a given amino acid to a different amino acid with similar biochemical properties (e.g. charge, hydrophobicity and size).

  8. Hydrophobe - Wikipedia

    en.wikipedia.org/wiki/Hydrophobe

    Water on hydrophobic surfaces will exhibit a high contact angle. Examples of hydrophobic molecules include the alkanes, oils, fats, and greasy substances in general. Hydrophobic materials are used for oil removal from water, the management of oil spills, and chemical separation processes to remove non-polar substances from polar compounds. [2]

  9. D-Amino acid - Wikipedia

    en.wikipedia.org/wiki/D-Amino_acid

    In this example, alanine is depicted in the zwitterionic form at physiological pH. D-Amino acids are amino acids where the stereogenic carbon alpha to the amino group has the D-configuration. For most naturally-occurring amino acids, this carbon has the L-configuration. D-Amino acids are occasionally found in nature as residues in proteins.