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Henry W. Orton

Researcher at Australian National University

Publications -  12
Citations -  273

Henry W. Orton is an academic researcher from Australian National University. The author has contributed to research in topics: Paramagnetism & Chemical shift. The author has an hindex of 6, co-authored 9 publications receiving 158 citations.

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Highly sensitive biosensors based on all-dielectric nanoresonators.

TL;DR: An all-dielectric sensing platform based on silicon nanodisks with strong optically-induced magnetic resonances is demonstrated, able to detect a concentration of streptavidin of as low as 10-10 M (mol L-1) or 5 ng mL-1, thus pushing the current detection limit by at least two orders of magnitudes.
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Paramagpy: software for fitting magnetic susceptibility tensors using paramagnetic effects measured in NMR spectra

TL;DR: Paramagpy as mentioned in this paper combines the functionalities of different currently available programs to support the fitting of magnetic susceptibility tensors using PCS, RDC, PRE and CCR data and molecular coordinates in Protein Data Bank (PDB) format, including a convenient graphical user interface.
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Paramagnetic Chemical Probes for Studying Biological Macromolecules

TL;DR: A comprehensive overview of the existing paramagnetic chemical probes, including chemical synthetic approaches, functional properties, and selected applications, can be found in this article , where the authors provide a comprehensive overview.
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Accurate Electron–Nucleus Distances from Paramagnetic Relaxation Enhancements

TL;DR: It is shown that PREs generated by lanthanides with anisotropic magnetic susceptibilities offer a route to accurate calibration-free distance measurements and is succeeded in measuring intramolecular PREs with unprecedented accuracy, resulting in distance predictions with a root-mean-square-deviation of <0.9 Å in the range 11-24 Å.
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Protein NMR resonance assignment without spectral analysis: 5D SOlid‐state Automated Projection SpectroscopY (SO‐APSY)

TL;DR: This work presents the first ultra-high dimensional implementation of this approach where 5D peak lists are reconstructed from a number of 2D projections for protein samples of different molecular size and aggregation state, featuring limited dispersion of chemical shifts or inhomogeneous broadenings.