I think a few pictures may provide a glimpse about the complexity here.
Yet the NMR spectrum of a given sample - say of an amino acid (building block for proteins) - already looks differently for scrutinizing the either peripheral hydrogens, the backbone of carbon atoms, or nitrogens. You basically probe your sample for specific atoms of a kind ( isotopes) and their nearest chemical environment. NMR spectroscopy typically characterizes probes soluted, keeping the molecules of interest (smaller ones, or large proteins) basically intact, without fragmentation.And if the molecules of interest are embedded in a matrix (e.g., a serum, a tissue), identification of this molecules by MS becomes even more complex. Depending on the ionization technique applied, the eventually intensity of these individual signals will vary. There are techniques keeping the molecules almost intact (softer ionization techniques, used for example in MS-mapping of tissues), and others (electon impact ionization) where the molecules are intentionally shattered into many differently sized fragments. mass spectroscopy typically relies on fragmenting the molecules in question, and then separates these then charged fragments by their mass/charge ratio.This is, at least in part, why chemists working in (especially, but not limited to) organic sythesis use these and additional ones to get a sufficiently "rounded picture" about the substances analyzed, putting the information each technique provides together. The techniques are quite different by their underlying principles. Sorry, but in my opinion this endeavour is unlikely to be successful.
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