When.com Web Search

  1. Ads

    related to: positive charged amino acids

Search results

  1. Results From The WOW.Com Content Network
  2. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    In a similar fashion, proteins that have to bind to positively charged molecules have surfaces rich in negatively charged amino acids such as glutamate and aspartate, while proteins binding to negatively charged molecules have surfaces rich in positively charged amino acids like lysine and arginine.

  3. Histone octamer - Wikipedia

    en.wikipedia.org/wiki/Histone_octamer

    All four of the core histone amino acid sequences contain between 20 and 24% of lysine and arginine and the size or the protein ranges between 11400 and 15400 daltons, making them relatively small, yet highly positively charged proteins. [6] High content of positively charged amino acids allow them to closely associate with negatively charged ...

  4. Histone H2B - Wikipedia

    en.wikipedia.org/wiki/Histone_H2B

    Histone tails and their function in chromatin formation. Histone H2B is a lightweight structural protein made of 126 amino acids. [2] Many of these amino acids have a positive charge at cellular pH, which allows them to interact with the negatively charged phosphate groups in DNA. [3]

  5. Histidine - Wikipedia

    en.wikipedia.org/wiki/Histidine

    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 protonated), classifying it as a ...

  6. Amine - Wikipedia

    en.wikipedia.org/wiki/Amine

    3) are the most common positively charged moieties in proteins, specifically in the amino acid lysine. [20] The anionic polymer DNA is typically bound to various amine-rich proteins. [ 21 ] Additionally, the terminal charged primary ammonium on lysine forms salt bridges with carboxylate groups of other amino acids in polypeptides , which is one ...

  7. Histone - Wikipedia

    en.wikipedia.org/wiki/Histone

    Salt bridges and hydrogen bonds between side chains of basic amino acids (especially lysine and arginine) and phosphate oxygens on DNA Helix-dipoles form alpha-helixes in H2B, H3, and H4 cause a net positive charge to accumulate at the point of interaction with negatively charged phosphate groups on DNA

  8. Histone acetylation and deacetylation - Wikipedia

    en.wikipedia.org/wiki/Histone_acetylation_and_de...

    The regulatory mechanism is thought to be twofold. Lysine is an amino acid with a positive charge when unmodified. Lysines on the amino terminal tails of histones have a tendency to weaken the chromatin's overall structure. Addition of an acetyl group, which carries a negative charge, effectively removes the positive charge and hence, reduces ...

  9. Leucine - Wikipedia

    en.wikipedia.org/wiki/Leucine

    Leucine (symbol Leu or L) [3] is an essential amino acid that is used in the biosynthesis of proteins.Leucine is an α-amino acid, meaning it contains an α-amino group (which is in the protonated −NH 3 + form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO − form under biological conditions), and a side chain isobutyl group, making it a non ...