A 1D proton NMR spectrum can contain a great deal of information, including:
(a) chemical shifts (what types of protons you have);
(b) peak integrations (the number of each type of proton you have); and
(c) splitting patterns (how each type of proton is connected in the chain – i.e., what its neighbours are).
This is a wealth of information about molecular structure and, realistically, is why 1H NMR is such a tremendous characterization technique. However, if all three pieces of information are not taken into account simultaneously, OR, if overlap or spectral crowding somehow masks them, there can be errors in structural assignments. In order to help simplify and/or clarify spectral assignment, we can reach into our 2D NMR toolbox to help deconvolute the data!
I’ve already discussed the better-known homonuclear 2D experiment – the COSY, which correlates chemical shifts of nearby protons through their scalar couplings.
The less common JRES experiment (also introduced by Ernst in 1976)[1], on the other hand, separates the scalar coupling and the chemical shift from a particular resonance multiplet and projects these two orthogonal pieces of data onto two different axes. Multiplicity is displayed along f1 and chemical shift is displayed along f2. This helps to simplify and de-convolute insufficiently resolved data. Although this experiment can be used to resolve both heteronuclear (1H-X) and homonuclear (1H-1H) multiplicities, I will limit this discussion to homonuclear couplings.
In its simplest case, the JRES experiment is:
(a) an interscan relaxation delay
(b) a 90o pulse to induce transverse magnetization
(c) a time delay (t1/2), which is incremented on successive iterations of the sequence, that allows evolution of chemical shift and coupling constants
(d) a 180o pulse to flip spins
(e) a second time delay (t1/2), also incremented, during which evolution under chemical shifts (but not under J-couplings) is refocused
(f) FID detection