I need to write a review about dynamic range in non-gel based proteomics approach, but I am not understanding the difference between dynamic range in gel-based and non-gel based approach.
There will be a dynamic range difference between gel-based and non-gel based approaches if there are differences in the fractionation degree prior to MS analysis.
In order to alter the dynamic range in your system one usually performs fractionation. This can be done is different ways:
- Protein fractionation (isoelectric focusing, PAGE, RP-LC, gel filtration)
- peptide fractionation ( isoelectric focusing, strong anion exchange, strong cation exchange,other of the exchange type, longer RP-LC gradients)
- MS based fractionation (gas-phase fractionation; http://link.springer.com/protocol/10.1007%2F978-1-59745-028-7_15).
The combination of different levels of these fractionation step alters the dynamic range.
There are several good review that you can use as templates for your work. I would recommend "Overcoming the dynamic range problem in mass spectrometry-based shotgun proteomics" http://informahealthcare.com/doi/abs/10.1586/14789450.3.6.611 (an older one) and "Separation methodology to improve proteome coverage depth" http://informahealthcare.com/doi/abs/10.1586/14789450.2014.919862 (a newer one)
Both are through Informa Healthcare to which most institutions do not have access so you should contact the authors directly and ask them for a copy.