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Default Multi-Quantum Chemical Exchange Saturation Transfer NMR to Quantify Symmetrical Exchange: Application to Rotational Dynamics of the Guanidinium Group in Arginine Side Chains.

Multi-Quantum Chemical Exchange Saturation Transfer NMR to Quantify Symmetrical Exchange: Application to Rotational Dynamics of the Guanidinium Group in Arginine Side Chains.

Related Articles Multi-Quantum Chemical Exchange Saturation Transfer NMR to Quantify Symmetrical Exchange: Application to Rotational Dynamics of the Guanidinium Group in Arginine Side Chains.

J Phys Chem Lett. 2020 Jun 16;:

Authors: Karunanithy G, Reinstein J, Hansen DF

Abstract
Chemical Exchange Saturation Transfer (CEST) NMR experiments have emerged as a powerful tool for characterizing dynamics in proteins. We show here that the CEST approach can be extended to systems with symmetrical exchange, where the NMR signals of all exchanging species are severely broadened. To achieve this, multi-quantum CEST (MQ-CEST) is introduced, where the CEST pulse is applied to a longitudinal multi-spin order density element and the CEST profiles encoded onto non-broadened nuclei. The MQ-CEST approach is demonstrated on the restricted rotation of guanidinium groups in arginine residues within proteins. These groups and their dynamics are essential for many enzymes and for non-covalent interactions through the formation of hydrogen bonds, salt-bridges and ?-stacking interactions and their rate of rotation is highly indicative of the extent of interactions formed. The MQ-CEST method is successfully applied to guanidinium groups in the 19 kDa L99A mutant of T4 Lysozyme.


PMID: 32543198 [PubMed - as supplied by publisher]



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