Asparagine deamidation and the role of higher order protein structure.
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.
Rivers
Jenny
J
Proteomics and Functional Genomics Group, Faculty of Veterinary Science, University of Liverpool, Liverpool, United Kingdom.
McDonald
Lucy
L
Edwards
Ian J
IJ
Beynon
Robert J
RJ
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
D000577:Amides; D011506:Proteins; D001216:Asparagine; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases