Top-down proteomics

Top-down proteomics is a method of protein identification that either uses an ion trapping mass spectrometer to store an isolated protein ion for mass measurement and tandem mass spectrometry (MS/MS) analysis[1][2] or other protein purification methods such as two-dimensional gel electrophoresis in conjunction with MS/MS.

[3] Top-down proteomics is capable of identifying and quantitating unique proteoforms through the analysis of intact proteins.

Effective fractionation is critical for sample handling before mass-spectrometry-based proteomics.

[7] Top-down MS (non-gel) proteomics interrogates protein structure through measurement of an intact mass followed by direct ion dissociation in the gas phase.

[8] Study One: Quantitation and Identification of Thousands of Human Proteoforms below 30 kDa Study Two: Combining high-throughput MALDI-TOF mass spectrometry and isoelectric focusing gel electrophoresis for virtual 2D gel-based proteomics