An NMR NOAH-supersequence is presented consisting of five CEST experiments for studying protein backbone and side-chain dynamics by ^(15)N-CEST, carbonyl-^(13)CO-CEST, aromatic-^(13)C(ar)-CEST, ^(13)C(?)-CEST, and methyl-^(13)C(met)-CEST. The new sequence acquires the data for these experiments in a fraction of the time required for the individual experiments, saving over four days of NMR time per sample.
[NMR paper] NOAH-(15N/13C)-CEST NMR supersequence for dynamics studies of biomolecules
NOAH-(15N/13C)-CEST NMR supersequence for dynamics studies of biomolecules
An NMR supersequence is introduced for the rapid acquisition of ^(15)N-CEST and methyl-^(13)C-CEST experiments in the same pulse sequence for applications to proteins. The high sensitivity and accuracy allows the simultaneous quantitative characterization of backbone and side-chain dynamics on the millisecond timescale ideal for routine screening for alternative protein states.
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07-29-2022 12:46 PM
Exchangeable deuterons introduce artifacts in amide 15 N CEST experiments used to study protein conformational exchange
Exchangeable deuterons introduce artifacts in amide 15 N CEST experiments used to study protein conformational exchange
Abstract
Protein molecules sample different conformations in solution and characterizing these conformations is crucial to understanding protein function. 15N CEST experiments are now routinely used to study slow conformational exchange of protein molecules between a ā??visibleā?? major state and ā??invisibleā?? minor states. These experiments have also been adapted to measure the solvent exchange rates of amide protons by exploiting...
[NMR paper] Residue Selective 15N CEST and CPMG Experiments for Studies of Millisecond Timescale Protein Dynamics
Residue Selective 15N CEST and CPMG Experiments for Studies of Millisecond Timescale Protein Dynamics
Publication date: Available online 1 June 2018
Source:Journal of Magnetic Resonance</br>
Author(s): Xiaogang Niu, Jienv Ding, Wenbo Zhang, Qianwen Li, Yunfei Hu, Changwen Jin</br>
Proteins are intrinsically dynamic molecules and undergo exchanges among multiple conformations to perform biological functions. The CPMG relaxation dispersion and CEST experiments are two important solution NMR techniques for characterizing the conformational exchange processes...
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06-03-2018 01:00 AM
Longitudinal relaxation optimized amide 1 H-CEST experiments for studying slow chemical exchange processes in fully protonated proteins
Longitudinal relaxation optimized amide 1 H-CEST experiments for studying slow chemical exchange processes in fully protonated proteins
Abstract
Chemical Exchange Saturation Transfer (CEST) experiments are increasingly used to study slow timescale exchange processes in biomolecules. Although 15N- and 13C-CEST have been the approaches of choice, the development of spin state selective 1H-CEST pulse sequences that separate the effects of chemical and dipolar exchange significantly increases the utility of 1H-based experiments. Pulse schemes have been...
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03-30-2017 06:42 PM
[NMR paper] "Invisible" Conformers of an Antifungal Disulfide Protein Revealed by Constrained Cold and Heat Unfolding, CEST-NMR Experiments, and Molecular Dynamics Calculations.
"Invisible" Conformers of an Antifungal Disulfide Protein Revealed by Constrained Cold and Heat Unfolding, CEST-NMR Experiments, and Molecular Dynamics Calculations.
Related Articles "Invisible" Conformers of an Antifungal Disulfide Protein Revealed by Constrained Cold and Heat Unfolding, CEST-NMR Experiments, and Molecular Dynamics Calculations.
Chemistry. 2015 Feb 12;
Authors: Fizil Į, Gįspįri Z, Barna T, Marx F, Batta G
Abstract
Transition between conformational states in proteins is being recognized as a possible key factor...
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02-14-2015 03:52 PM
Triple resonance-based 13 C Ī± and 13 C Ī² CEST experiments for studies of ms timescale dynamics in proteins
Triple resonance-based 13 C Ī± and 13 C Ī² CEST experiments for studies of ms timescale dynamics in proteins
Abstract
A pair of triple resonance based CEST pulse schemes are presented for measuring 13CĪ± and 13CĪ² chemical shifts of sparsely populated and transiently formed conformers that are invisible to traditional NMR experiments. CEST profiles containing dips at resonance positions of 13CĪ± or 13CĪ² spins of major (ground) and minor (excited) conformers are obtained in a pseudo 3rd dimension that is generated by quantifying modulations of cross...
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10-28-2014 02:42 PM
[NMR paper] A Comparative CEST NMR Study of Slow Conformational Dynamics of Small GTPases Complexed with GTP and GTP Analogues.
A Comparative CEST NMR Study of Slow Conformational Dynamics of Small GTPases Complexed with GTP and GTP Analogues.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles A Comparative CEST NMR Study of Slow Conformational Dynamics of Small GTPases Complexed with GTP and GTP Analogues.
Angew Chem Int Ed Engl. 2013 Aug 22;
Authors: Long D, Marshall CB, Bouvignies G, Mazhab-Jafari MT, Smith MJ, Ikura M, Kay LE
Abstract
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ARCHE-NOAH: NMR supersequence with five different CEST experiments for studying protein conformational dynamics
Linear Mode
