Unbiased measurements of reconstruction fidelity of sparsely sampled magnetic resonance spectra.
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The application of sparse-sampling techniques to NMR data acquisition would benefit from reliable quality measurements for reconstructed spectra. We introduce a pair of noise-normalized measurements, and , for differentiating inadequate modelling from overfitting. While and can be used jointly for methods that do not enforce exact agreement between the back-calculated time domain and the original sparse data, the cross-validation measure is applicable to all reconstruction algorithms. We show that the fidelity of reconstruction is sensitive to changes in and that model overfitting results in elevated and reduced spectral quality.
Published Version (Please cite this version)10.1038/ncomms12281
Publication InfoCoggins, Brian E; Wu, Qinglin; & Zhou, Pei (2016). Unbiased measurements of reconstruction fidelity of sparsely sampled magnetic resonance spectra. Nat Commun, 7. pp. 12281. 10.1038/ncomms12281. Retrieved from https://hdl.handle.net/10161/13065.
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Professor of Biochemistry
Protein-protein interactions play a pivotal role in the regulation of various cellular processes. The formation of higher order protein complexes is frequently accompanied by extensive structural remodeling of the individual components, varying from domain re-orientation to induced folding of unstructured elements. Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful tool for macromolecular structure determination in solution. It has the unique advantage of being capable of elucidati