enow.com Web Search

Search results

  1. Results from the WOW.Com Content Network
  2. Hydrophobicity scales - Wikipedia

    en.wikipedia.org/wiki/Hydrophobicity_scales

    Different organic solvents are most widely used to mimic the protein interior. However, organic solvents are slightly miscible with water and the characteristics of both phases change making it difficult to obtain pure hydrophobicity scale. [3] Nozaki and Tanford proposed the first major hydrophobicity scale for nine amino acids. [15]

  3. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    Structure of a typical L-alpha-amino acid in the "neutral" form. Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. [1] Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. [2]

  4. 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 ...

  5. Organic chemistry - Wikipedia

    en.wikipedia.org/wiki/Organic_chemistry

    Neutral organic compounds tend to be hydrophobic; that is, they are less soluble in water than inorganic solvents. Exceptions include organic compounds that contain ionizable groups as well as low molecular weight alcohols, amines, and carboxylic acids where hydrogen bonding occurs. Otherwise, organic compounds tend to dissolve in organic ...

  6. Hopp–Woods scale - Wikipedia

    en.wikipedia.org/wiki/Hopp–Woods_scale

    The Hopp–Woods hydrophilicity scale of amino acids is a method of ranking the amino acids in a protein according to their water solubility in order to search for surface locations on proteins, and especially those locations that tend to form strong interactions with other macromolecules such as proteins, DNA, and RNA. [1] [2]

  7. Tyrosine - Wikipedia

    en.wikipedia.org/wiki/Tyrosine

    Phosphorylation of these three amino acids' moieties (including tyrosine) creates a negative charge on their ends, that is greater than the negative charge of the only negatively charged aspartic and glutamic acids. Phosphorylated proteins keep these same properties—which are useful for more reliable protein-protein interactions—by means of ...

  8. IUPAC nomenclature of organic chemistry - Wikipedia

    en.wikipedia.org/wiki/IUPAC_nomenclature_of...

    In chemical nomenclature, the IUPAC nomenclature of organic chemistry is a method of naming organic chemical compounds as recommended [1] [2] by the International Union of Pure and Applied Chemistry (IUPAC). It is published in the Nomenclature of Organic Chemistry (informally called the Blue Book). [3]

  9. Chaotropic agent - Wikipedia

    en.wikipedia.org/wiki/Chaotropic_agent

    A chaotropic agent is a substance which disrupts the structure of, and denatures, macromolecules such as proteins and nucleic acids (e.g. DNA and RNA).Chaotropic solutes increase the entropy of the system by interfering with intermolecular interactions mediated by non-covalent forces such as hydrogen bonds, van der Waals forces, and hydrophobic effects.