Direct mass spectrometric analysis of intact proteins of the yeast large ribosomal subunit using capillary LC/FTICR

Sang Won Lee, Scott J. Berger, Suzana Martinović, Ljiljana Paša-Tolić, Gordon A. Anderson, Yufeng Shen, Rui Zhao, Richard D. Smith

Research output: Contribution to journalArticlepeer-review

166 Citations (Scopus)


Electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry coupled with capillary reverse-phase liquid chromatography was used to characterize intact proteins from the large subunit of the yeast ribosome. High mass measurement accuracy, achieved by "mass locking" with an internal standard from a dual electrospray ionization source, allowed identification of ribosomal proteins. Analyses of the intact proteins revealed information on cotranslational and posttranslational modifications of the ribosomal proteins that included loss of the initiating methionine, acetylation, methylation, and proteolytic maturation. High-resolution separations permitted differentiation of protein isoforms having high structural similarity as well as proteins from their modified forms, facilitating unequivocal assignments. The study identified 42 of the 43 core large ribosomal subunit proteins and 58 (of 64 possible) core large subunit protein isoforms having unique masses in a single analysis. These results demonstrate the basis for the high-throughput analyses of complex mixtures of intact proteins, which we believe will be an important complement to other approaches for defining protein modifications and their changes resulting from physiological processes or environmental perturbations.

Original languageEnglish
Pages (from-to)5942-5947
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number9
Publication statusPublished - 2002 Apr 30

ASJC Scopus subject areas

  • General


Dive into the research topics of 'Direct mass spectrometric analysis of intact proteins of the yeast large ribosomal subunit using capillary LC/FTICR'. Together they form a unique fingerprint.

Cite this