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  2. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    Similar to acetylation. Instead of a simple methyl group, the myristoyl group has a tail of 14 hydrophobic carbons, which make it ideal for anchoring proteins to cellular membranes. The C-terminal carboxylate group of a polypeptide can also be modified, e.g., Fig. 3 C-terminal amidation. amination (see Figure)

  3. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    The image above contains clickable links This diagram (which is interactive) of protein structure uses PCNA as an example. (Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule.

  4. Ribbon diagram - Wikipedia

    en.wikipedia.org/wiki/Ribbon_diagram

    Ribbon diagrams, also known as Richardson diagrams, are 3D schematic representations of protein structure and are one of the most common methods of protein depiction used today. The ribbon depicts the general course and organisation of the protein backbone in 3D and serves as a visual framework for hanging details of the entire atomic structure ...

  5. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    The oxidation pathway starts with the removal of the amino group by a transaminase; the amino group is then fed into the urea cycle. The other product of transamidation is a keto acid that enters the citric acid cycle. [79] Glucogenic amino acids can also be converted into glucose, through gluconeogenesis. [80]

  6. Threonine - Wikipedia

    en.wikipedia.org/wiki/Threonine

    Threonine (symbol Thr or T) [2] is an amino acid that is used in the biosynthesis of proteins.It contains an α-amino group (which is in the protonated −NH + 3 form when dissolved in water), a carboxyl group (which is in the deprotonated −COO − form when dissolved in water), and a side chain containing a hydroxyl group, making it a polar, uncharged amino acid.

  7. 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 ...

  8. Tryptophan - Wikipedia

    en.wikipedia.org/wiki/Tryptophan

    Like other amino acids, tryptophan is a zwitterion at physiological pH where the amino group is protonated (– NH + 3; pK a = 9.39) and the carboxylic acid is deprotonated ( –COO −; pK a = 2.38). [5] Humans and many animals cannot synthesize tryptophan: they need to obtain it through their diet, making it an essential amino acid.

  9. N-terminus - Wikipedia

    en.wikipedia.org/wiki/N-terminus

    Each amino acid has an amine group and a carboxylic group. Amino acids link to one another by peptide bonds which form through a dehydration reaction that joins the carboxyl group of one amino acid to the amine group of the next in a head-to-tail manner to form a polypeptide chain. The chain has two ends – an amine group, the N-terminus, and ...