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Aspartyl-tRNA Synthetase-Induced Aspartylation of Proteins: a Fingerprint Approach to Map Accessible Domains in Protein
Book chapter

Aspartyl-tRNA Synthetase-Induced Aspartylation of Proteins: a Fingerprint Approach to Map Accessible Domains in Protein

H Mejdoub, D Kern, R Giege, Y Boulanger and J Reinbolt
Advanced Methods in Protein Microsequence Analysis, pp.291-299
Springer Berlin Heidelberg
1986
DOI: https://doi.org/10.1007/978-3-642-71534-1_24

Abstract

Amino Alcohol Degradation Step Label Peptide Aspartic Acid Aspartic Acid Residue
Aspartic acid can be covalently linked to yeast aspartyl-tRNA synthetase and to other proteins in the absence of tRNA, under conditions where the synthetase activates the amino acid into aspartyl-adenylate, i.e., in the presence of ATP and MgCl2 [1,2]. The aspartyl adenylate is poorly bound to the enzyme.

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