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  2. 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. [85] Glucogenic amino acids can also be converted into glucose, through gluconeogenesis. [86]

  3. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    The two ends of the polypeptide chain are referred to as the carboxyl terminus (C-terminus) and the amino terminus (N-terminus) based on the nature of the free group on each extremity. Counting of residues always starts at the N-terminal end (NH 2 -group), which is the end where the amino group is not involved in a peptide bond.

  4. Arginine - Wikipedia

    en.wikipedia.org/wiki/Arginine

    Arginine is the amino acid with the formula (H 2 N)(HN)CN(H)(CH 2) 3 CH(NH 2)CO 2 H. The molecule features a guanidino group appended to a standard amino acid framework. At physiological pH, the carboxylic acid is deprotonated (−CO 2 −) and both the amino and guanidino groups are protonated, resulting in a cation.

  5. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    The N-terminal amino group of a polypeptide can be modified covalently, e.g., Fig. 1 N-terminal acetylation. acetylation (=) The positive charge on the N-terminal amino group may be eliminated by changing it to an acetyl group (N-terminal blocking). formylation (=)

  6. Protein - Wikipedia

    en.wikipedia.org/wiki/Protein

    [29]: 31 The end with a free amino group is known as the N-terminus or amino terminus, whereas the end of the protein with a free carboxyl group is known as the C-terminus or carboxy terminus (the sequence of the protein is written from N-terminus to C-terminus, from left to right). [citation needed]

  7. 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 ...

  8. 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 ...

  9. Lysine - Wikipedia

    en.wikipedia.org/wiki/Lysine

    Lysine (symbol Lys or K) [2] is an α-amino acid that is a precursor to many proteins.Lysine contains an α-amino group (which is in the protonated −NH + 3 form when the lysine is dissolved in water at physiological pH), an α-carboxylic acid group (which is in the deprotonated −COO − form when the lysine is dissolved in water at physiological pH), and a side chain (CH 2) 4 NH 2 (which ...