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  2. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    Structure of a typical L-alpha-amino acid in the "neutral" form. Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. [1] Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. [2] Only these 22 appear in the genetic code of life ...

  3. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    Protein sequence is typically notated as a string of letters, listing the amino acids starting at the amino-terminal end through to the carboxyl-terminal end. Either a three letter code or single letter code can be used to represent the 22 naturally encoded amino acids, as well as mixtures or ambiguous amino acids (similar to nucleic acid ...

  4. Protein - Wikipedia

    en.wikipedia.org/wiki/Protein

    The amino acids in a polypeptide chain are linked by peptide bonds between amino and carboxyl group. An individual amino acid in a chain is called a residue, and the linked series of carbon, nitrogen, and oxygen atoms are known as the main chain or protein backbone.

  5. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers – specifically polypeptides – formed from sequences of amino acids, which are the monomers of the polymer. A single amino acid monomer may also be called a residue, which indicates a

  6. 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 ...

  7. Amphoterism - Wikipedia

    en.wikipedia.org/wiki/Amphoterism

    The water molecule is amphoteric in aqueous solution. It can either gain a proton to form a hydronium ion H 3 O +, or else lose a proton to form a hydroxide ion OH −. [5] Another possibility is the molecular autoionization reaction between two water molecules, in which one water molecule acts as an acid and another as a base.

  8. Asparagine - Wikipedia

    en.wikipedia.org/wiki/Asparagine

    Asparagine (symbol Asn or N [2]) is an α-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), an α-carboxylic acid group (which is in the deprotonated −COO − form under biological conditions), and a side chain carboxamide, classifying it as a polar (at physiological pH), aliphatic ...

  9. Sørensen formol titration - Wikipedia

    en.wikipedia.org/wiki/Sørensen_formol_titration

    The liberated hydrochloric acid is then titrated with the base and the amount of ammonium salt used can be determined. With an amino acid the formaldehyde reacts with the amino group to form a methylene amino (R-N=CH 2) group. The remaining acidic carboxylic acid group can then again be titrated with base. [3]