Journal
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
Volume 11, Issue 14, Pages 5649-5654Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpclett.0c01322
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Funding
- BBSRC [BB/R000255/1]
- Wellcome Trust [101569/z/13/z, FC001029]
- University of Oxford Wellcome Institutional Strategic Support Fund
- Engineering and Physical Sciences Research Council [EP/R029849/1]
- Cancer Research UK [FC001029]
- UK Medical Research Council [FC001029]
- Leverhulme Trust [RPG-2016-268]
- Wellcome Trust [101569/Z/13/Z] Funding Source: Wellcome Trust
- BBSRC [BB/R000255/1] Funding Source: UKRI
- EPSRC [EP/R029849/1] Funding Source: UKRI
- MRC [MC_U117533887] Funding Source: UKRI
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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, multiquantum CEST (MQ-CEST) is introduced, where the CEST pulse is applied to a longitudinal multispin order density element and the CEST profiles are encoded onto nonbroadened 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 noncovalent interactions through the formation of hydrogen bonds, salt-bridges, and pi-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.
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