Registration and Grouping Algorithms in Protein NMR Derived Peak Lists and Their Application in Protein NMR Reference Correction

Registration and Grouping Algorithms in Protein NMR Derived Peak Lists and Their Application in Protein NMR Reference Correction

Nuclear magnetic resonance spectroscopy of proteins (protein NMR) is a powerful analytical technique for studying structure and dynamics of proteins. Almost all aspects of protein NMR have been accelerated by the development of software tools that enable the analysis of NMR spectral data and its utilization in studying protein structure and dynamics. This includes software for raw NMR processing, spectral visualization, protein resonance assignment, and structure determination. However, full automation of protein NMR data analysis is still a work in progress and data analysis still requires an expert NMR spectroscopist utilizing an array of software tools.

While manual resonance assignment with spectral visualization software is tedious and can take a significant amount of time, a variety of automated and semi-automated assignment programs have been developed to facilitate the protein resonance assignment process, specifically for solution and solid-state NMR. But one of the historical problems that has limited the use of automated and semi-automated protein resonance assignment tools along with other analyses of NMR peak lists is the requirement that users specify uniform match tolerances to perform spin systems grouping and linking or rely on default uniform match tolerance values provided by the tool.