Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra.

By M. Ottiger, Frank Delaglio, A. Bax. 1998

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Citations in the corpus

• De novo protein design by deep network hallucination (2020, methodology): “RDC data collection on both isotropic and partially aligned samples was performed at 600 MHz using a 2D interleaved 15 N-1 H-HSQC IPAP experiment to measure couplings 37 .”
• Structural Basis for Sequence Specific DNA Binding and Protein Dimerization of HOXA13 (2011, methodology): “Onebond HN RDCs were recorded using the in-phase/anti-phase pulse sequence [43], with 512 complex t1 ((15)N) points for both the isotropic and anisotropic samples.”
• Structural Polymorphism of 441-Residue Tau at Single Residue Resolution (2009, methodology): “One-bond N-H RDCs (DNH) were determined by using an inphaseantiphase (IPAP)-HSQC [73].”
• Automated protein fold determination using a minimal NMR constraint strategy (2003, methodology): “One bond N–H and C -C splittings were measured on the free and aligned samples using 2D IPAP N-H HSQC (Ottiger et al. 1998) and 3D C -coupled HNCO (Tjandra and Bax 1997).”