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Updated: Feb 19, 2026

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy NMR and Microscale Thermophoresis MST
Published on: November 2, 2018
Dipolar filtered magic-sandwich-echoes as a tool for probing molecular motions using time domain NMR
Jefferson G Filgueiras1, Uilson B da Silva1, Giovanni Paro1
1Instituto de Física de São Carlos, Universidade de São Paulo, P.O. Box 369, São Carlos, 13560-970 SP, Brazil.
Abstract:
We present a simple 1H NMR approach for characterizing intermediate to fast regime molecular motions using 1H time-domain NMR at low magnetic field. The method is based on a Goldmann Shen dipolar filter (DF) followed by a Mixed Magic Sandwich Echo (MSE). The dipolar filter suppresses the signals arising from molecular segments presenting sub kHz mobility, so only signals from mobile segments are detected. Thus, the temperature dependence of the signal intensities directly evidences the onset of molecular motions with rates higher than kHz. The DF-MSE signal intensity is described by an analytical function based on the Anderson Weiss theory, from where parameters related to the molecular motion (e.g. correlation times and activation energy) can be estimated when performing experiments as function of the temperature. Furthermore, we propose the use of the Tikhonov regularization for estimating the width of the distribution of correlation times.
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