The development of Fourier transform NMR in the mid 1960' s, did parallel processing of the collection of NMR data, increased the signal/noise ratio by two orders of magnitude and made it possible to record the proton NMR spectra of small proteins which contain hundreds of resonances. The assignment of these resonances then became a challenge, which was solved with the development of two-dimensional Fourier transform NMR, also called 2D NMR. This article describes the initial start and development of the various methods of 2D NMR leading to structure determination of proteins in solution and two Nobel Prizes.