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  2. Hydrophile - Wikipedia

    en.wikipedia.org/wiki/Hydrophile

    Hydrophilic molecules (and portions of molecules) can be contrasted with hydrophobic molecules (and portions of molecules). In some cases, both hydrophilic and hydrophobic properties occur in a single molecule. An example of these amphiphilic molecules is the lipids that comprise the cell membrane.

  3. Hydrophobicity scales - Wikipedia

    en.wikipedia.org/wiki/Hydrophobicity_scales

    When consecutively measuring amino acids of a protein, changes in value indicate attraction of specific protein regions towards the hydrophobic region inside lipid bilayer. The hydrophobic or hydrophilic character of a compound or amino acid is its hydropathic character, [1] hydropathicity, or hydropathy.

  4. Hydrophobe - Wikipedia

    en.wikipedia.org/wiki/Hydrophobe

    Dew drop on a hydrophobic leaf surface Cutting a water droplet using a superhydrophobic knife on superhydrophobic surfaces Water drops on the hydrophobic surface of grass In chemistry , hydrophobicity is the chemical property of a molecule (called a hydrophobe ) that is seemingly repelled from a mass of water . [ 1 ]

  5. Hydrophobic effect - Wikipedia

    en.wikipedia.org/wiki/Hydrophobic_effect

    The hydrophobic effect depends on the temperature, which leads to "cold denaturation" of proteins. [19] The hydrophobic effect can be calculated by comparing the free energy of solvation with bulk water. In this way, the hydrophobic effect not only can be localized but also decomposed into enthalpic and entropic contributions. [3]

  6. 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 ...

  7. Transmembrane domain - Wikipedia

    en.wikipedia.org/wiki/Transmembrane_domain

    A transmembrane domain (TMD, TM domain) is a membrane-spanning protein domain.TMDs may consist of one or several alpha-helices or a transmembrane beta barrel.Because the interior of the lipid bilayer is hydrophobic, the amino acid residues in TMDs are often hydrophobic, although proteins such as membrane pumps and ion channels can contain polar residues.

  8. Interbilayer forces in membrane fusion - Wikipedia

    en.wikipedia.org/wiki/Interbilayer_Forces_in...

    Hydrophobic forces are the attractive entropic forces between any two hydrophobic groups in aqueous media, e.g. the forces between two long hydrocarbon chains in aqueous solutions. The magnitude of these forces depends on the hydrophobicity of the interacting groups as well as the distance separating them (they are found to decrease roughly ...

  9. Lyotropic liquid crystal - Wikipedia

    en.wikipedia.org/wiki/Lyotropic_liquid_crystal

    Such molecules comprise a hydrophilic (literally 'water-loving') head-group (which may be ionic or non-ionic) attached to a hydrophobic ('water-hating') group. The micro-phase segregation of two incompatible components on a nanometer scale results in different type of solvent-induced extended anisotropic [ 3 ] arrangement, depending on the ...