enow.com Web Search

Search results

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

    en.wikipedia.org/wiki/Histidine

    Histidine ball and stick model spinning. Histidine (symbol His or H) [2] is an essential 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), a carboxylic acid group (which is in the deprotonated –COO − form under biological conditions), and an imidazole side chain (which is partially ...

  3. His-tag - Wikipedia

    en.wikipedia.org/wiki/His-tag

    The sample and subsequent buffers are manually poured into the column and collected at the bottom end after flowing through the resin bed (in light blue at the base of the column). A polyhistidine-tag , best known by the trademarked name His-tag , is an amino acid motif in proteins that typically consists of at least six histidine ( His ...

  4. Histidine (data page) - Wikipedia

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

    ^a CID 71083 from PubChem (D-histidine) ^a CID 6274 from PubChem (L-histidine) This page was last edited on 12 April 2023, at 11:40 (UTC). Text is ...

  5. Catalytic triad - Wikipedia

    en.wikipedia.org/wiki/Catalytic_triad

    The triad of cytomegalovirus protease [b] uses histidine as both the acid and base triad members. Removing the acid histidine results in only a 10-fold activity loss (compared to >10,000-fold when aspartate is removed from chymotrypsin). This triad has been interpreted as a possible way of generating a less active enzyme to control cleavage ...

  6. 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 ...

  7. Hydrophobicity scales - Wikipedia

    en.wikipedia.org/wiki/Hydrophobicity_scales

    Polar chemical groups, such as OH group in methanol do not cause the hydrophobic effect. However, a pure hydrocarbon molecule, for example hexane, cannot accept or donate hydrogen bonds to water. Introduction of hexane into water causes disruption of the hydrogen bonding network between water molecules.

  8. Chemical polarity - Wikipedia

    en.wikipedia.org/wiki/Chemical_polarity

    These effects add as vectors to make the overall molecule polar. A polar molecule has a net dipole as a result of the opposing charges (i.e. having partial positive and partial negative charges) from polar bonds arranged asymmetrically. Water (H 2 O) is an example of a polar molecule since it has a slight positive charge on one side and a ...

  9. Non-covalent interaction - Wikipedia

    en.wikipedia.org/wiki/Non-covalent_interaction

    A dipole-induced dipole interaction (Debye force) is due to the approach of a molecule with a permanent dipole to another non-polar molecule with no permanent dipole. This approach causes the electrons of the non-polar molecule to be polarized toward or away from the dipole (or "induce" a dipole) of the approaching molecule. [13]