title: Asparagine deamidation and the role of higher order protein structure.
abstract: The 'protein world' exhibits additional complexity caused by post-translational modifications. One such process is nonenzymic deamidation of asparagine which is controlled partly by primary sequence, but also higher order protein structure. We have studied the deamidation of an N-terminal peptide in muscle glyceraldehyde 3-phosphate dehydrogenase to relate three-dimensional structure, proteolysis, and deamidation. This work has significant consequences for identification of proteins using peptide mass fingerprinting.
authors.affiliation: Proteomics and Functional Genomics Group, Faculty of Veterinary Science, University of Liverpool, Liverpool, United Kingdom.
authors.forename: Jenny
authors.initials: J
authors.lastname: Rivers
authors.forename: Lucy
authors.initials: L
authors.lastname: McDonald
authors.forename: Ian J
authors.initials: IJ
authors.lastname: Edwards
authors.forename: Robert J
authors.initials: RJ
authors.lastname: Beynon
mesh_terms: D000577:Amides / Q000737:chemistry*; D000595:Amino Acid Sequence; D001216:Asparagine / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D004951:Esterification; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry; D006868:Hydrolysis; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid
chemical_list: D000577:Amides; D011506:Proteins; D001216:Asparagine; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases