The enzymatic cleavage ofN-acetyl-2-azido-2-deoxy-α-d-neuraminic acid in the probe of the NMR spectrometer allows the accumulation of1H NMR spectra of the released a anomer of the N-acetyl-d-neuraminic acid before it mutarotates to the β anomer. The analysis and computer simulation of the spectra yield the1H NMR data set of chemical shifts and coupling constants ofN-acetyl-α-d-neuraminic acid. Using this data set, configuration and conformation in solution are discussed by comparing it with the1H NMR data set of the β anomer, the structure of which is known from an X-ray study.