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  2. Glycine - Wikipedia

    en.wikipedia.org/wiki/Glycine

    Glycine (symbol Gly or G; [6] / ˈ ɡ l aɪ s iː n / ⓘ) [7] is an amino acid that has a single hydrogen atom as its side chain. It is the simplest stable amino acid (carbamic acid is unstable). Glycine is one of the proteinogenic amino acids. It is encoded by all the codons starting with GG (GGU, GGC, GGA, GGG). [8]

  3. Functional group - Wikipedia

    en.wikipedia.org/wiki/Functional_group

    For example, sugar dissolves in water because both share the hydroxyl functional group (−OH) and hydroxyls interact strongly with each other. Plus, when functional groups are more electronegative than atoms they attach to, the functional groups will become polar, and the otherwise nonpolar molecules containing these functional groups become ...

  4. List of water-miscible solvents - Wikipedia

    en.wikipedia.org/wiki/List_of_water-miscible...

    The following compounds are liquid at room temperature and are completely miscible with water; ... pyridine: 110-86-1 C 4 H 8 O 2 S: sulfolane: 126-33-0 (CH 2) 4 O ...

  5. Non-covalent interaction - Wikipedia

    en.wikipedia.org/wiki/Non-covalent_interaction

    The hydrophobic effect is the desire for non-polar molecules to aggregate in aqueous solutions in order to separate from water. [22] This phenomenon leads to minimum exposed surface area of non-polar molecules to the polar water molecules (typically spherical droplets), and is commonly used in biochemistry to study protein folding and other ...

  6. Pyridine - Wikipedia

    en.wikipedia.org/wiki/Pyridine

    Pyridine is a basic heterocyclic organic compound with the chemical formula C 5 H 5 N. It is structurally related to benzene, with one methine group (=CH−) replaced by a nitrogen atom (=N−). It is a highly flammable, weakly alkaline, water-miscible liquid with a distinctive, unpleasant fish

  7. Salt bridge (protein and supramolecular) - Wikipedia

    en.wikipedia.org/wiki/Salt_bridge_(protein_and...

    In chemistry, a salt bridge is a combination of two non-covalent interactions: hydrogen bonding and ionic bonding (Figure 1). Ion pairing is one of the most important noncovalent forces in chemistry, in biological systems, in different materials and in many applications such as ion pair chromatography. It is a most commonly observed ...

  8. Chemical polarity - Wikipedia

    en.wikipedia.org/wiki/Chemical_polarity

    Bonds can fall between one of two extremes – completely nonpolar or completely polar. A completely nonpolar bond occurs when the electronegativities are identical and therefore possess a difference of zero. A completely polar bond is more correctly called an ionic bond, and occurs when the difference

  9. Talk:Glycine - Wikipedia

    en.wikipedia.org/wiki/Talk:Glycine

    "The polar, uncharged amino acids except for glycine contain R groups, that can form hydrogen bonds with water. Thus, these amino acids are usually more soluble that non-polar amino acids." It continues later on "Glycine, the simplest amino acid, has only a single hydrogen for an R group, and this hydrogen is not a good hydrogen bond former.