title: Hirudin: a family of iso-proteins. Isolation and sequence determination of new hirudins.
abstract: A recent NMR study of hirudin conformation in solution reveals a large extent of the tertiary structure of the inhibitor [2]. This model exhibits a highly packed core and two other extended wings-like domains. One of these domains centred at Gly (position 34) shows an accumulation of amino acid mutations, insertions, deletions located at an exposed position. This may represent evolutionary optimisation of the thrombin-binding site.
authors: Hoechst A.G., Frankfurt, FRG.
authors: D
authors: D
authors: Tripier
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000235:genetics; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D006629:Hirudins / Q000302:isolation & purification*; D007865:Leeches / Q000032:analysis; D008969:Molecular Sequence Data; D009154:Mutation; D010446:Peptide Fragments / Q000302:isolation & purification; D013917:Thrombin / Q000037:antagonists & inhibitors
chemical_list: D000596:Amino Acids; D006629:Hirudins; D010446:Peptide Fragments; D013917:Thrombin