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  2. Valine - Wikipedia

    en.wikipedia.org/wiki/Valine

    Valine ball and stick model spinning. Valine (symbol Val or V) [4] is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated −NH 3 + form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO − form under biological conditions), and a side chain isopropyl group, making it a non-polar ...

  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. Hydrophobicity scales - Wikipedia

    en.wikipedia.org/wiki/Hydrophobicity_scales

    Polar chemical groups, such as OH group in methanol do not cause the hydrophobic effect. However, a pure hydrocarbon molecule, for example hexane, cannot accept or donate hydrogen bonds to water. Introduction of hexane into water causes disruption of the hydrogen bonding network between water molecules.

  5. Alpha helix - Wikipedia

    en.wikipedia.org/wiki/Alpha_helix

    The alpha helix is also commonly called a: Pauling–Corey–Branson α-helix (from the names of three scientists who described its structure); 3.6 13-helix because there are 3.6 amino acids in one ring, with 13 atoms being involved in the ring formed by the hydrogen bond (starting with amidic hydrogen and ending with carbonyl oxygen)

  6. 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] In contrast, hydrophiles are ...

  7. Globin - Wikipedia

    en.wikipedia.org/wiki/Globin

    The most famous mutation in the globin fold is a change from glutamate to valine in one chain of the hemoglobin molecule. This mutation creates a "hydrophobic patch" on the protein surface that promotes intermolecular aggregation, the molecular event that gives rise to sickle-cell disease. [citation needed]

  8. Beta sheet - Wikipedia

    en.wikipedia.org/wiki/Beta_sheet

    However, several notable exceptions include the Outer Surface Protein A (OspA) variants [7] and the Single Layer β-sheet Proteins (SLBPs) [11] which contain single-layer β-sheets in the absence of a traditional hydrophobic core. These β-rich proteins feature an extended single-layer β-meander β-sheets that are primarily stabilized via ...

  9. Valinomycin - Wikipedia

    en.wikipedia.org/wiki/Valinomycin

    Valinomycin is a dodecadepsipeptide, that is, it is made of twelve alternating amino acids and esters to form a macrocyclic molecule. The twelve carbonyl groups are essential for the binding of metal ions, and also for solvation in polar solvents.