[NMR paper] A Unique and Simple Approach to Improve Sensitivity in (15)N-NMR Relaxation Measurements for NH?? Groups: Application to a Protein-DNA Complex.
Related ArticlesA Unique and Simple Approach to Improve Sensitivity in (15)N-NMR Relaxation Measurements for NH?? Groups: Application to a Protein-DNA Complex.
Molecules. 2017 Aug 15;22(8):
Authors: Nguyen D, Lokesh GLR, Volk DE, Iwahara J
Abstract
NMR spectroscopy is a powerful tool for research on protein dynamics. In the past decade, there has been significant progress in the development of NMR methods for studying charged side chains. In particular, NMR methods for lysine side-chain NH?? groups have been proven to be powerful for investigating the dynamics of hydrogen bonds or ion pairs that play important roles in biological processes. However, relatively low sensitivity has been a major practical issue in NMR experiments on NH?? groups. In this paper, we present a unique and simple approach to improve sensitivity in (15)N relaxation measurements for NH?? groups. In this approach, the efficiency of coherence transfers for the desired components are maximized, whereas undesired anti-phase or multi-spin order components are purged through pulse schemes and rapid relaxation. For lysine side-chain NH?? groups of a protein-DNA complex, we compared the data obtained with the previous and new pulse sequences under the same conditions and confirmed that the (15)N relaxation parameters were consistent for these datasets. While retaining accuracy in measuring (15)N relaxation, our new pulse sequences for NH?? groups allowed an 82% increase in detection sensitivity of (15)N longitudinal and transverse relaxation measurements.
[NMR paper] An Integrated Approach to Unique NMR Assignment of Methionine Methyl Resonances in Proteins.
An Integrated Approach to Unique NMR Assignment of Methionine Methyl Resonances in Proteins.
Related Articles An Integrated Approach to Unique NMR Assignment of Methionine Methyl Resonances in Proteins.
Anal Chem. 2017 Feb 07;89(3):1610-1616
Authors: Yu F, Qiao J, Robblee J, Tsao D, Anderson J, Capila I
Abstract
The application of methyl nuclear magnetic resonance (NMR) spectroscopy in protein side-chain structural studies offers unique advantages of greater peak sensitivity, even for high-molecular-weight proteins....
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02-18-2017 11:35 AM
[NMR paper] Cross-Correlated Relaxation of Dipolar Coupling and Chemical-Shift Anisotropy in Magic-Angle Spinning R1? NMR Measurements: Application to Protein Backbone Dynamics Measurements.
Cross-Correlated Relaxation of Dipolar Coupling and Chemical-Shift Anisotropy in Magic-Angle Spinning R1? NMR Measurements: Application to Protein Backbone Dynamics Measurements.
Cross-Correlated Relaxation of Dipolar Coupling and Chemical-Shift Anisotropy in Magic-Angle Spinning R1? NMR Measurements: Application to Protein Backbone Dynamics Measurements.
J Phys Chem B. 2016 Aug 8;
Authors: Kurauskas V, Weber E, Hessel A, Ayala I, Marion D, Schanda P
Abstract
Transverse relaxation rate measurements in MAS solid-state NMR...
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08-09-2016 02:42 PM
[NMR paper] Increasing the sensitivity of NMR diffusion measurements by paramagnetic longitudinal relaxation enhancement, with application to ribosome-nascent chain complexes.
Increasing the sensitivity of NMR diffusion measurements by paramagnetic longitudinal relaxation enhancement, with application to ribosome-nascent chain complexes.
Related Articles Increasing the sensitivity of NMR diffusion measurements by paramagnetic longitudinal relaxation enhancement, with application to ribosome-nascent chain complexes.
J Biomol NMR. 2015 Aug 8;
Authors: Chan SH, Waudby CA, Cassaignau AM, Cabrita LD, Christodoulou J
Abstract
The translational diffusion of macromolecules can be examined non-invasively by...
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08-09-2015 05:01 PM
Increasing the sensitivity of NMR diffusion measurements by paramagnetic longitudinal relaxation enhancement, with application to ribosomeâ??nascent chain complexes
Increasing the sensitivity of NMR diffusion measurements by paramagnetic longitudinal relaxation enhancement, with application to ribosomeâ??nascent chain complexes
Abstract
The translational diffusion of macromolecules can be examined non-invasively by stimulated echo (STE) NMR experiments to accurately determine their molecular sizes. These measurements can be important probes of intermolecular interactions and protein folding and unfolding, and are crucial in monitoring the integrity of large macromolecular assemblies...
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08-08-2015 12:17 PM
Paramagnetic relaxation enhancement to improve sensitivity of fast NMR methods: application to intrinsically disordered proteins
Paramagnetic relaxation enhancement to improve sensitivity of fast NMR methods: application to intrinsically disordered proteins
Abstract We report enhanced sensitivity NMR measurements of intrinsically disordered proteins in the presence of paramagnetic relaxation enhancement (PRE) agents such as Ni2+-chelated DO2A. In proton-detected 1H-15N SOFAST-HMQC and carbon-detected (H-flip)13CO-15N experiments, faster longitudinal relaxation enables the usage of even shorter interscan delays. This results in higher NMR signal intensities per units of experimental time, without adverse line...
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10-21-2011 10:04 PM
NMR as a Unique Tool in Assessment and Complex Determination of Weak Protein-Protein Interactions.
NMR as a Unique Tool in Assessment and Complex Determination of Weak Protein-Protein Interactions.
NMR as a Unique Tool in Assessment and Complex Determination of Weak Protein-Protein Interactions.
Top Curr Chem. 2011 Aug 2;
Authors: Vinogradova O, Qin J
Protein-protein interactions are crucial for a wide variety of biological processes. These interactions range from high affinity (K (d) < nM) to very low affinity (K (d) > mM). While much is known about the nature of high affinity protein complexes, our knowledge about structural characteristics...
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08-03-2011 12:00 PM
Combination of NMR spectroscopy and X-ray crystallography offers unique advantages for elucidation of the structural basis of protein complex assembly.
Combination of NMR spectroscopy and X-ray crystallography offers unique advantages for elucidation of the structural basis of protein complex assembly.
Combination of NMR spectroscopy and X-ray crystallography offers unique advantages for elucidation of the structural basis of protein complex assembly.
Sci China Life Sci. 2011 Feb;54(2):101-11
Authors: Feng W, Pan L, Zhang M
NMR spectroscopy and X-ray crystallography are two premium methods for determining the atomic structures of macro-biomolecular complexes. Each method has unique strengths and...
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02-15-2011 07:17 PM
[NMR paper] A simple approach to analyzing protein side-chain dynamics from 13C NMR relaxation da
A simple approach to analyzing protein side-chain dynamics from 13C NMR relaxation data.
Related Articles A simple approach to analyzing protein side-chain dynamics from 13C NMR relaxation data.
J Magn Reson. 1998 Feb;130(2):329-34
Authors: Daragan VA, Mayo KH
A simple approach to deriving motional dynamics information of protein and peptide side chains by using 13C NMR relaxation data is presented. By using linear approximation of internal rotational correlation functions, simple equations for relating side-chain conformation, bond rotational...