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 Wüth rich 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.
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