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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. It is the simplest stable amino acid.

  3. Non-covalent interaction - Wikipedia

    en.wikipedia.org/wiki/Non-covalent_interaction

    Hydrogen-bonding-in-water. A hydrogen bond (H-bond), is a specific type of interaction that involves dipole–dipole attraction between a partially positive hydrogen atom and a highly electronegative, partially negative oxygen, nitrogen, sulfur, or fluorine atom (not covalently bound to said hydrogen atom).

  4. Covalent bond - Wikipedia

    en.wikipedia.org/wiki/Covalent_bond

    A double bond between two given atoms consists of one σ and one π bond, and a triple bond is one σ and two π bonds. [8] Covalent bonds are also affected by the electronegativity of the connected atoms which determines the chemical polarity of the bond. Two atoms with equal electronegativity will make nonpolar covalent bonds such as H–H.

  5. Chemical polarity - Wikipedia

    en.wikipedia.org/wiki/Chemical_polarity

    The terms "polar" and "nonpolar" are usually applied to covalent bonds, that is, bonds where the polarity is not complete. To determine the polarity of a covalent bond using numerical means, the difference between the electronegativity of the atoms is used.

  6. Chemical bond - Wikipedia

    en.wikipedia.org/wiki/Chemical_bond

    Molecules that are formed primarily from non-polar covalent bonds are often immiscible in water or other polar solvents, but much more soluble in non-polar solvents such as hexane. A polar covalent bond is a covalent bond with a significant ionic character. This means that the two shared electrons are closer to one of the atoms than the other ...

  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. 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)

  9. Intramolecular force - Wikipedia

    en.wikipedia.org/wiki/Intramolecular_force

    In a true covalent bond, the electrons are shared evenly between the two atoms of the bond; there is little or no charge separation. Covalent bonds are generally formed between two nonmetals. There are several types of covalent bonds: in polar covalent bonds , electrons are more likely to be found around one of the two atoms, whereas in ...