enow.com Web Search

Search results

  1. Results from the WOW.Com Content Network
  2. 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 ...

  3. 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.

  4. Valine - Wikipedia

    en.wikipedia.org/wiki/Valine

    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 aliphatic amino acid.

  5. Proteinogenic amino acid - Wikipedia

    en.wikipedia.org/wiki/Proteinogenic_amino_acid

    These are the biggest amino acids. Like isoleucine, leucine, and valine, these are hydrophobic and tend to orient towards the interior of the folded protein molecule. Phenylalanine can be converted into tyrosine. Glycine: G Gly Because of the two hydrogen atoms at the α carbon, glycine is not optically active. It is the smallest amino acid ...

  6. Alpha helix - Wikipedia

    en.wikipedia.org/wiki/Alpha_helix

    The first and especially the fourth residues (known as the a and d positions) are almost always hydrophobic; the fourth residue is typically leucine – this gives rise to the name of the structural motif called a leucine zipper, which is a type of coiled-coil. These hydrophobic residues pack together in the interior of the helix bundle.

  7. Beta sheet - Wikipedia

    en.wikipedia.org/wiki/Beta_sheet

    The side chains from the amino acid residues found in a β-sheet structure may also be arranged such that many of the adjacent sidechains on one side of the sheet are hydrophobic, while many of those adjacent to each other on the alternate side of the sheet are polar or charged (hydrophilic), [21] which can be useful if the sheet is to form a ...

  8. Dying To Be Free - The Huffington Post

    projects.huffingtonpost.com/dying-to-be-free...

    There’s no single explanation for why addiction treatment is mired in a kind of scientific dark age, why addicts are denied the help that modern medicine can offer. Family doctors tend to see addicts as a nuisance or a liability and don’t want them crowding their waiting rooms. In American culture, self-help runs deep.

  9. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    Glycine and proline are strongly present within low complexity regions of both eukaryotic and prokaryotic proteins, whereas the opposite is the case with cysteine, phenylalanine, tryptophan, methionine, valine, leucine, isoleucine, which are highly reactive, or complex, or hydrophobic. [40] [42] [43]