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Updated: Jul 24, 2025

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Observation of magnetic structural universality and jamming transition with NMR
Alexander Ruh1, Philipp Emerich1, Harald Scherer2
1Medical Physics, Department of Radiology, Faculty of Medicine, University of Freiburg, Freiburg, Germany.
Abstract:
Nuclear magnetic resonance (NMR) has been instrumental in deciphering the structure of proteins. Here we show that transverse NMR relaxation, through its time-dependent relaxation rate, is distinctly sensitive to the structure of complex materials or biological tissues at the mesoscopic scale, from micrometers to tens of micrometers. Based on the ideas of universality, we show analytically and numerically that the time-dependent transverse relaxation rate approaches its long-time limit in a power-law fashion, with the dynamical exponent reflecting the universality class of mesoscopic magnetic structure. The spectral line shape acquires the corresponding non-analytic power law singularity at zero frequency. We experimentally detect the change in the dynamical exponent as a result of the transition into maximally random jammed state characterized by hyperuniform correlations. The relation between relaxational dynamics and magnetic structure opens the way for noninvasive characterization of porous media, complex materials and biological tissues.
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