Analysis of methylation, acetylation, and other modifications in bacterial ribosomal proteins.
A wide variety of post-translational modifications of expressed proteins are known to occur in living organisms (1). Although their presence in an organism cannot be predicted from the genome, these modifications can play critical roles in protein structure and function. The identification of post-translational modifications can be critical in understanding the functions of proteins involved in important biological pathways and mass spectrometry offers a fast, accurate method for observing them. This chapter describes the procedure for analyzing ribosomal proteins of Escherichia coli by matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry and Caulobacter crescentus ribosomal proteins by electrospray quadrupole time-of-flight (ESI-QTOF) mass spectrometry.
Arnold
Randy J
RJ
Department of Chemistry, Indiana University, Bloomington, IN, USA.
Running
William
W
Reilly
James P
JP
D000107:Acetylation; D002853:Chromatography, Liquid; D029968:Escherichia coli Proteins / Q000378:metabolism*; D008745:Methylation; D012269:Ribosomal Proteins / Q000378:metabolism*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D029968:Escherichia coli Proteins; D012269:Ribosomal Proteins