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.
[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
Multiple frequency saturation pulses reduce CEST acquisition time for quantifying conformational exchange in biomolecules
Multiple frequency saturation pulses reduce CEST acquisition time for quantifying conformational exchange in biomolecules
Abstract
Exchange between conformational states is required for biomolecular catalysis, allostery, and folding. A variety of NMR experiments have been developed to quantify motional regimes ranging from nanoseconds to seconds. In this work, we describe an approach to speed up the acquisition of chemical exchange saturation transfer (CEST) experiments that are commonly used to probe millisecond to second conformational exchange in...
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05-24-2018 12:57 AM
A new class of CEST experiment based on selecting different magnetization components at the start and end of the CEST relaxation element: an application to 1 H CEST
A new class of CEST experiment based on selecting different magnetization components at the start and end of the CEST relaxation element: an application to 1 H CEST
Abstract
Chemical exchange saturation transfer (CEST) experiments are becoming increasingly popular for investigating biomolecular exchange dynamics with rates on the order of approximately 50â??500Â*sâ??1 and a rich toolkit of different methods has emerged over the past few years. Typically, experiments are based on the evolution of longitudinal magnetization, or in some cases two-spin...
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01-19-2018 08:57 PM
Triple resonance-based 13 C α and 13 C β CEST experiments for studies of ms timescale dynamics in proteins
Triple resonance-based 13 C α and 13 C β CEST experiments for studies of ms timescale dynamics in proteins
Abstract
A pair of triple resonance based CEST pulse schemes are presented for measuring 13Cα and 13Cβ chemical shifts of sparsely populated and transiently formed conformers that are invisible to traditional NMR experiments. CEST profiles containing dips at resonance positions of 13Cα or 13Cβ 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] High-Dimensional NMR Spectra for Structural Studies of Biomolecules.
High-Dimensional NMR Spectra for Structural Studies of Biomolecules.
High-Dimensional NMR Spectra for Structural Studies of Biomolecules.
Chemphyschem. 2013 Jun 21;
Authors: Kazimierczuk K, Stanek J, Zawadzka-Kazimierczuk A, Ko?mi?ski W
Abstract
Recent developments in the acquisition and processing of NMR data sets facilitate the recording of ultra-high-resolution NMR spectra in a reasonable time. The new experiments allow easy resonance assignment for folded and unfolded proteins, as well as the precise determination of spectral...
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06-26-2013 09:39 AM
Exceeding the limit of dynamics studies on biomolecules using high spin-lock field strengths with a cryogenically cooled probehead
Exceeding the limit of dynamics studies on biomolecules using high spin-lock field strengths with a cryogenically cooled probehead
Publication year: 2012
Source:Journal of Magnetic Resonance</br>
David Ban, Alvar D. Gossert, Karin Giller, Stefan Becker, Christian Griesinger, Donghan Lee</br>
Internal motions in the microsecond timescale have been proposed to play an active part in a protein’s biological function. Nuclear magnetic resonance (NMR) relaxation dispersion is a robust method sensitive to this timescale with atomic resolution. However, due to technical...
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05-15-2012 06:40 PM
Dynamics of Biomolecules from Picoseconds to Seconds at Atomic Resolution
Dynamics of Biomolecules from Picoseconds to Seconds at Atomic Resolution
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 22 July 2011</br>
Dennis A., Torchia</br>
Although biomolecular dynamics has been investigated using NMR for at least 40 years, only in the past 20 years have internal motions been characterized at atomic resolution throughout proteins and nucleic acids. This development was made possible by multidimensional heteronuclear NMR approaches that provide near complete sequential signal assignments of...
NOAH-(15N/13C)-CEST NMR supersequence for dynamics studies of biomolecules
Linear Mode
