Table of Contents
International Journal of Proteomics
Volume 2013 (2013), Article ID 674282, 10 pages
Research Article

Quantitative Proteomics via High Resolution MS Quantification: Capabilities and Limitations

1Global Discovery and Development Statistics, Lilly Research Laboratories, Indianapolis, IN 46285, USA
2Lilly Corporate Center, DC 0720, Indianapolis, IN 46285, USA
3Translational Sciences, Lilly Research Laboratories, Indianapolis, IN 46285, USA

Received 15 October 2012; Accepted 6 February 2013

Academic Editor: Valerie Wasinger

Copyright © 2013 Richard E. Higgs et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Supplementary Material

Table S1: Instrument settings used for the multiple reaction monitoring (MRM) experiments.

Table S2: Parent and daughter ions used to quantify yeast enolase with the MRM experiments.

Table S3: Yeast enolase concentrations used in all experiments.

Table S4: Lookup table that can be used to identify the smallest number of isotopes in an isotope distribution in order to retain ∼75% of the total signal in the isotope distribution.

Figure S1: Retention time vs. dilutional optimal model R2 value demonstrating the effects of non-specific binding with a TFA/water background matrix.

  1. Supplementary Material