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  2. Methionine - Wikipedia

    en.wikipedia.org/wiki/Methionine

    Methionine (symbol Met or M) [3] (/ m ɪ ˈ θ aɪ ə n iː n /) [4] is an essential amino acid in humans.. As the precursor of other non-essential amino acids such as cysteine and taurine, versatile compounds such as SAM-e, and the important antioxidant glutathione, methionine plays a critical role in the metabolism and health of many species, including humans.

  3. Chemical polarity - Wikipedia

    en.wikipedia.org/wiki/Chemical_polarity

    A completely polar bond is more correctly called an ionic bond, and occurs when the difference between electronegativities is large enough that one atom actually takes an electron from the other. The terms "polar" and "nonpolar" are usually applied to covalent bonds, that is, bonds where the polarity is not complete. To determine the polarity ...

  4. Methionine (data page) - Wikipedia

    en.wikipedia.org/wiki/Methionine_(data_page)

    The complete data for Methionine. General information. Chemical formula: C 5 H 11 N O 2 S ... Hydrogen bond: donor - 2; ...

  5. Pi-interaction - Wikipedia

    en.wikipedia.org/wiki/Pi-interaction

    In chemistry, π-effects or π-interactions are a type of non-covalent interaction that involves π systems.Just like in an electrostatic interaction where a region of negative charge interacts with a positive charge, the electron-rich π system can interact with a metal (cationic or neutral), an anion, another molecule and even another π system. [1]

  6. Disulfide - Wikipedia

    en.wikipedia.org/wiki/Disulfide

    Since water molecules attack amide-amide hydrogen bonds and break up secondary structure, a disulfide bond stabilizes secondary structure in its vicinity. For example, researchers have identified several pairs of peptides that are unstructured in isolation, but adopt stable secondary and tertiary structure upon formation of a disulfide bond ...

  7. 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). It is not a covalent bond, but ...

  8. Intramolecular force - Wikipedia

    en.wikipedia.org/wiki/Intramolecular_force

    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 nonpolar covalent bonds, electrons are evenly shared. Homonuclear diatomic molecules are purely covalent.

  9. Metal ions in aqueous solution - Wikipedia

    en.wikipedia.org/wiki/Metal_ions_in_aqueous_solution

    The strength of the bonds between the metal ion and water molecules in the primary solvation shell increases with the electrical charge, z, on the metal ion and decreases as its ionic radius, r, increases. Aqua ions are subject to hydrolysis. The logarithm of the first hydrolysis constant is proportional to z 2 /r for most aqua ions.