Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data.

By J. Battiste, G. Wagner. Biochemistry, 2000

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Structural Polymorphism of 441-Residue Tau at Single Residue Resolution (2009, background): “These smoothed intensity ratios were linearly fit for the enhancement of the transverse relaxation rate by the unpaired electron [75].”
Determination of the three-dimensional structure of the Mrf2-DNA complex using paramagnetic spin labeling. (2007, methodology): “6, intermolecular distance constraints were calculated using Equations (1) and (2).”
NMR contributions to structural dynamics studies of intrinsically disordered proteins (2014, positive): “In the first approach PRE data are converted into distances using well-established methodology [28] that can subsequently be used in, for example, MD simulations to calculate conformational ensembles [29].”
Structural Mechanisms of Nucleosome Recognition by Linker Histones (2015, background): “spin labels on the NMR peak intensities of the methyl groups depend on their distances to the corresponding methyl groups of the globular domain in an inversely related manner (Battiste and Wagner, 2000).”
De novo protein structure determination using sparse NMR data (2000, background): “Using less information, low-resolution global folds can be obtained for large proteins that can greatly simplify resonance and constraint assignments (Venters et al., 1995; Rosen et al., 1996; Gardner et al., 1997; Battiste and Wagner, 2000).”