A study was conducted to demonstrate the use of NMR as a as a tool to determine the structures, folding behavior, dynamics, and interactions of plant proteins. Investigations revealed that one-dimensional (1D) spectra were useful for rapid characterization of the folding or structure of smaller proteins. Correct folding was associated with sharp spectral lines and good dispersion of the amide signals or the observation of some upfield-shifted methyl groups. Upfield or down field dispersion of the α-H shifts provided a measure of helical or β-sheet secondary structure. A quick measure of the folding of proteins was also obtained from the pattern of chemical shifts in two-dimensional (2D) HSQC spectra for larger proteins. This was conveniently done with 15N-labeled samples, but the sensitivity of modern instruments equipped with cryo-probes allowed 2D HSQC spectra to be recorded for natural abundance samples.