Application of Dirichlet process mixture model to the identification of spin systems in protein NMR spectra

Journal of Biomolecular NMR
Piotr KlukowskiMichal J Walczak

Abstract

Analysis of structure, function and interactions of proteins by NMR spectroscopy usually requires the assignment of resonances to the corresponding nuclei in protein. This task, although automated by methods such as FLYA or PINE, is still frequently performed manually. To facilitate the manual sequence-specific chemical shift assignment of complex proteins, we propose a method based on Dirichlet process mixture model (DPMM) that performs automated matching of groups of signals observed in NMR spectra to corresponding nuclei in protein sequence. The model has been extensively tested on 80 proteins retrieved from the BMRB database and has shown superior performance to the reference method.

References

Mar 23, 2002·Protein Science : a Publication of the Protein Society·Yunjun Wang, Oleg Jardetzky
Feb 12, 2004·Journal of Biomolecular NMR·Hunter N B MoseleyGaetano T Montelione
Aug 20, 2004·Methods in Molecular Biology·Peter Güntert
Oct 3, 2006·Journal of Biomolecular NMR·Ivano BertiniGeorgios A Spyroulias
Nov 7, 2007·Nucleic Acids Research·Eldon L UlrichJohn L Markley
Feb 18, 2011·Journal of Bioinformatics and Computational Biology·Babak AlipanahiMing Li
Jul 17, 2012·Journal of the American Chemical Society·Elena Schmidt, Peter Güntert
Aug 8, 2013·Nucleic Acids Research·Thomas AeschbacherMario Schubert
Mar 17, 2018·Bioinformatics·Piotr KlukowskiMichal J Walczak

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