Annals of Biomedical Engineering

, Volume 42, Issue 2, pp 299–311 | Cite as

Chemical Tools for Temporally and Spatially Resolved Mass Spectrometry-Based Proteomics

  • Kai P. Yuet
  • David A. Tirrell


Accurate measurements of the abundances, synthesis rates and degradation rates of cellular proteins are critical for understanding how cells and organisms respond to changes in their environments. Over the past two decades, there has been increasing interest in the use of mass spectrometry for proteomic analysis. In many systems, however, protein diversity as well as cell and tissue heterogeneity limit the usefulness of mass spectrometry-based proteomics. As a result, researchers have had difficulty in systematically identifying proteins expressed within specified time intervals, or low abundance proteins expressed in specific tissues or in a few cells in complex microbial systems. In this review, we present recently-developed tools and strategies that probe these two subsets of the proteome: proteins synthesized during well-defined time intervals—temporally resolved proteomics—and proteins expressed in predetermined cell types, cells or cellular compartments—spatially resolved proteomics—with a focus on chemical and biological mass spectrometry-based methodologies.


Protein synthesis BONCAT SILAC APEX 



Work at Caltech on non-canonical amino acid tagging is supported by National Institutes of Health grant NIH R01 GM062523 and by the Institute for Collaborative Biotechnologies through grant W911NF-09-0001 from U.S. Army Research Office.


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Copyright information

© Biomedical Engineering Society 2013

Authors and Affiliations

  1. 1.Division of Chemistry and Chemical EngineeringCalifornia Institute of TechnologyPasadenaUSA

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