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Updated: Sep 23, 2025

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
Published on: November 1, 2024
An efficient combination of BEST and NUS methods in multidimensional NMR spectroscopy for high throughput analysis of
Veera Mohana Rao Kakita1, Mandar Bopardikar2, Vaibhav Kumar Shukla1
1UM-DAE Centre for Excellence in Basic Sciences, University of Mumbai Kalina Campus, Santacruz Mumbai 400 098 India.
Abstract:
Application of Non Uniform Sampling (NUS) along with Band-selective Excitation Short-Transient (BEST) NMR experiments has been demonstrated for obtaining the important residue-specific atomic level backbone chemical shift values in short durations of time. This application has been demonstrated with both well-folded (ubiquitin) and unfolded (α-synuclein) proteins alike. With this strategy, the experiments required for determining backbone chemical shifts can be performed very rapidly, i.e., in ∼2 hours of spectrometer time, and this data can be used to calculate the backbone folds of proteins using well established algorithms. This will be of great value for structural proteomic investigations on one hand, where the speed of structure determination is a limiting factor and for application in the study of slow kinetic processes involving proteins, such as fibrillization, on the other hand.
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