Top Down Mass Spectrometry is a technique to characterize the entire sequence of a protein with its related modifications. This service line is tailored to the comprehensive analysis of semi-pure proteins with minimal non-target protein contamination. Examples of good candidates for this approach include recombinantly-expressed proteins, in vitro enzyme assay experiments and the characterization of bioactive peptides.

Related Publications

Hong SH, Ntai I, Haimovich AD, Kelleher NL, Isaacs FJ, Jewett MC “Cell-free protein synthesis from a release factor 1 deficient Escherichia coli activates efficient and multiple site-specific nonstandard amino acid incorporation.” ACS Synth Biol, 2014, 3(6) p. 398-409.

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Siuti N, Kelleher NL “Decoding protein modifications using top-down mass spectrometry.” Nat Methods, 2007, 4(10) p. 817-21.

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Savaryn JP, Catherman AD, Thomas PM, Abecassis MM, Kelleher NL “The emergence of top-down proteomics in clinical research.” Genome Med, 2013, 5(6) p. 53.

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Pricing

https://proteomics.northwestern.edu/services/rates/

Instruments Used

Orbitrap Elite

Q Exactive HF

Q Exactive UHMR