Nuclear magnetic resonance (NMR) spectroscopy and X-ray crystallography are two experimental techniques used to determine the three-dimensional structures of proteins. NMR spectroscopy has the unique ability to capture proteins in vivo. Currently, protein structure determination by NMR follows the procedure proposed by Kurt Wüthrich in 1986 . This procedure consists of peak picking, resonance assignment, nuclear overhauser effect (NOE) assignment and structure calculation steps. Among the four steps, peak picking is time consuming and requires extensive expert knowledge. Computational methods designed to automate and improve this step are still needed. The inputs to the peak picking problem are an NMR spectrum or a set of spectra, whereas the outputs are the lists of peaks (signals) identified from these spectra.