Protein Structure Determination Using Molecular Fragment Replacement and NMR Dipolar Couplings

By Frank Delaglio, A. Kontaxis, Ad Bax. 2000

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Automated protein fold determination using a minimal NMR constraint strategy (2003, methodology): “In fact, RDC data have been used as primary NMR constraints for rapid determination of protein global folds (Delaglio et al. 2000; Fowler et al. 2000; Hus et al. 2000; Andrec et al. 2001, 2002; Rohl and Baker 2002).”
Consistent blind protein structure generation from NMR chemical shift data (2008, methodology): “…of the protein structure database (PDB) for fragments approximately compatible with these couplings and the experimental chemical shifts then yields substructures that subsequently can be assembled using a molecular fragment replacement (MFR) method into a model for the target protein (11).”
Chemical shift-based methods in NMR structure determination (2018, methodology): “Year Description (method) Reference 1993 NOE assignment and structure refinement approach (ASNO) [213] 1995 Introduction of ambiguous NOE distance restraints [144] 1997 Protein structure determination methods using fragment assembly (Ab initio) [57,58] 1997 NMR structure calculation using ambiguous ”