The short timescale of interconversion precludes the separation of conformational isomers in most cases. Atropisomers are conformational isomers which can be separated due to restricted rotation. The equilibrium between conformational isomers can be observed using a variety of spectroscopic techniques.
Protein folding also generates stable conformational isomers which can be observed. The Karplus equation relates the dihedral angle of vicinal protons to their J-coupling constants as measured by NMR. The equation aids in the elucidation of protein folding as well as the conformations of other rigid aliphatic molecules. Protein side chains exhibit rotamers, whose distribution is determined by their steric interaction with different conformations of the backbone. This is evident from statistical analysis of the conformations of protein side chains in the Backbone-dependent rotamer library.
In cyclohexane derivatives, the two chair conformers interconvert with rapidly at room temperature, with cyclohexane itself undergoing the ring-flip at a rates of approximately 10 ring-flips/sec, with an overall energy barrier of 10 kcal/mol (42 kJ/mol), which precludes their separation at ambient temperatures. However, at low temperatures below the coalescence point one can directly monitor the equilibrium by NMR spectroscopy and by dynamic, temperature dependent NMR spectroscopy the barrier interconversion.
The dynamics of conformational (and other kinds of) isomerism can be monitored by NMR spectroscopy at varying temperatures. The technique applies to barriers of 8–14 kcal/mol, and species exhibiting such dynamics are often called "fluxional".
Besides NMR spectroscopy, IR spectroscopy is used to measure conformer ratios. For the axial and equatorial conformer of bromocyclohexane, ν differs by almost 50 cm.