[NMR paper] 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 ArticlesMulti-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]
3-O-Methyl- d -glucose mutarotation and proton exchange rates assessed by 13 C, 1 H NMR and by chemical exchange saturation transfer and spin lock measurements
3-O-Methyl- d -glucose mutarotation and proton exchange rates assessed by 13 C, 1 H NMR and by chemical exchange saturation transfer and spin lock measurements
Abstract
3-O-Methyl-d-glucose (3OMG) was recently suggested as an agent to image tumors using chemical exchange saturation transfer (CEST) MRI. To characterize the properties of 3OMG in solution, the anomeric equilibrium and the mutarotation rates of 3OMG were studied by 1H and 13C NMR. This information is essential in designing the in vivo CEST experiments. At room temperature, the ratio...
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11-25-2018 06:02 AM
[NMR paper] A (13)C-detected (15)N double-quantum NMR experiment to probe arginine side-chain guanidinium (15)N(?) chemical shifts.
A (13)C-detected (15)N double-quantum NMR experiment to probe arginine side-chain guanidinium (15)N(?) chemical shifts.
A (13)C-detected (15)N double-quantum NMR experiment to probe arginine side-chain guanidinium (15)N(?) chemical shifts.
J Biomol NMR. 2017 Nov 10;:
Authors: Mackenzie HW, Hansen DF
Abstract
Arginine side-chains are often key for enzyme catalysis, protein-ligand and protein-protein interactions. The importance of arginine stems from the ability of the terminal guanidinium group to form many key interactions,...
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11-13-2017 12:45 AM
A 13 C-detected 15 N double-quantum NMR experiment to probe arginine side-chain guanidinium 15 N η chemical shifts
A 13 C-detected 15 N double-quantum NMR experiment to probe arginine side-chain guanidinium 15 N η chemical shifts
Abstract
Arginine side-chains are often key for enzyme catalysis, proteinâ??ligand and proteinâ??protein interactions. The importance of arginine stems from the ability of the terminal guanidinium group to form many key interactions, such as hydrogen bonds and salt bridges, as well as its perpetual positive charge. We present here an arginine 13Cζ-detected NMR experiment in which a double-quantum coherence involving the two 15Nη nuclei...
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11-10-2017 05:01 PM
[NMR paper] Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR.
Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR.
Related Articles Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR.
Chem Commun (Camb). 2017 Aug 25;:
Authors: Gerecht K, Figueiredo AM, Hansen DF
Abstract
Arginine residues are imperative for many active sites and protein-interaction interfaces. A new NMR-based method is presented to determine the rotational dynamics around the N?-C? bond of...
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08-26-2017 03:38 PM
Probing conformational dynamics in biomolecules via chemical exchange saturation transfer: a primer
Probing conformational dynamics in biomolecules via chemical exchange saturation transfer: a primer
Abstract
Although Chemical Exchange Saturation Transfer (CEST) type NMR experiments have been used to study chemical exchange processes in molecules since the early 1960s, there has been renewed interest in the past several years in using this approach to study biomolecular conformational dynamics. The methodology is particularly powerful for the study of sparsely populated, transiently formed conformers that are recalcitrant to investigation using...
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03-19-2017 10:38 PM
[U. of Ottawa NMR Facility Blog] CEST - Chemical Exchange Saturation Transfer
CEST - Chemical Exchange Saturation Transfer
Chemical Exchange Saturation Transfer (CEST) is a technique where one resonance, in slow exchange with a second resonance, is saturated with a selective low power pulse followed by a hard non-selective 90° pulse. The intensity of the second resonance is then diminished due to the transfer of saturation from the first resonance as the result of chemical exchange. The figure below demonstrates this for a 25 mM solution of salicylic acid in H2O/D2O buffered at pH 7. ...
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04-22-2016 08:45 PM
[NMR paper] Rapid Determination of Fast Protein Dynamics from NMR Chemical Exchange Saturation Transfer Data.
Rapid Determination of Fast Protein Dynamics from NMR Chemical Exchange Saturation Transfer Data.
Related Articles Rapid Determination of Fast Protein Dynamics from NMR Chemical Exchange Saturation Transfer Data.
Angew Chem Int Ed Engl. 2016 Jan 28;
Authors: Gu Y, Hansen AL, Peng Y, Brüschweiler R
Abstract
Functional motions of (15) N-labeled proteins can be monitored by solution NMR spin relaxation experiments over a broad range of timescales. These experiments however typically take of the order of several days to a week per...
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01-30-2016 09:13 PM
[NMR paper] Probing Slow Chemical Exchange at Carbonyl Sites in Proteins by Chemical Exchange Saturation Transfer NMR Spectroscopy.
Probing Slow Chemical Exchange at Carbonyl Sites in Proteins by Chemical Exchange Saturation Transfer NMR Spectroscopy.
Probing Slow Chemical Exchange at Carbonyl Sites in Proteins by Chemical Exchange Saturation Transfer NMR Spectroscopy.
Angew Chem Int Ed Engl. 2013 Feb 28;
Authors: Vallurupalli P, Kay LE
Abstract
Seeing the invisible: A 13 CO NMR chemical exchange saturation transfer (CEST) experiment for the study of "invisible" excited protein states with lifetimes on the order of 5-50 ms has been developed. The 13 CO chemical...
Multi-Quantum Chemical Exchange Saturation Transfer NMR to Quantify Symmetrical Exchange: Application to Rotational Dynamics of the Guanidinium Group in Arginine Side Chains.
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