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  2. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    A rare exception to the dominance of α-amino acids in biology is the β-amino acid beta alanine (3-aminopropanoic acid), which is used in plants and microorganisms in the synthesis of pantothenic acid (vitamin B 5), a component of coenzyme A. [77]

  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. N-terminus - Wikipedia

    en.wikipedia.org/wiki/N-terminus

    The N-terminus (also known as the amino-terminus, NH 2-terminus, N-terminal end or amine-terminus) is the start of a protein or polypeptide, referring to the free amine group (-NH 2) located at the end of a polypeptide. Within a peptide, the amine group is bonded to the carboxylic group of another amino acid

  5. Biomolecule - Wikipedia

    en.wikipedia.org/wiki/Biomolecule

    Amino acids contain both amino and carboxylic acid functional groups. (In biochemistry , the term amino acid is used when referring to those amino acids in which the amino and carboxylate functionalities are attached to the same carbon, plus proline which is not actually an amino acid).

  6. Sequence motif - Wikipedia

    en.wikipedia.org/wiki/Sequence_motif

    In biology, a sequence motif is a nucleotide or amino-acid sequence pattern that is widespread and usually assumed to be related to biological function of the macromolecule. For example, an N -glycosylation site motif can be defined as Asn, followed by anything but Pro, followed by either Ser or Thr, followed by anything but Pro residue .

  7. Protein domain - Wikipedia

    en.wikipedia.org/wiki/Protein_domain

    The primary structure (string of amino acids) of a protein ultimately encodes its uniquely folded three-dimensional (3D) conformation. [20] The most important factor governing the folding of a protein into 3D structure is the distribution of polar and non-polar side chains. [ 21 ]

  8. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    The active site consists of amino acid residues that form temporary bonds with the substrate, the binding site, and residues that catalyse a reaction of that substrate, the catalytic site. Although the active site occupies only ~10–20% of the volume of an enzyme, [ 1 ] : 19 it is the most important part as it directly catalyzes the chemical ...

  9. Nirenberg and Matthaei experiment - Wikipedia

    en.wikipedia.org/wiki/Nirenberg_and_Matthaei...

    The experiments used mixtures with all 20 amino acids. For each individual experiment, 19 amino acids were "cold" (nonradioactive), and one was "hot" (radioactively tagged with 14 C so they could detect the tagged amino acid later). They varied the "hot" amino acid in each round of the experiment, seeking to determine which amino acids would be ...