The possibility of using selectively incorporated ^(19)F nuclei for NMR spectroscopic studies has retrieved increasing interest in recent years. The high gyromagnetic ratio of ^(19)F and its absence in native biomolecular systems make this nucleus an interesting alternative to standard ¹H NMR spectroscopy. Here we show how we can attach a label, carrying a ^(19)F atom, to protein tyrosines, through the use of a specific three component Mannich-type reaction. To validate the efficacy and the...
[NMR paper] Probing the Conformational States of Neurotensin Receptor 1 Variants*by NMR Site-Directed Methyl Labeling.
Probing the Conformational States of Neurotensin Receptor 1 Variants*by NMR Site-Directed Methyl Labeling.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7388-69-wiley-full-text.png Related Articles Probing the Conformational States of Neurotensin Receptor 1 Variants*by NMR Site-Directed Methyl Labeling.
Chembiochem. 2020 Sep 02;:
Authors: Goba I, Goricanec D, Schum D, Hillenbrand M, Plückthun A, Hagn F
Abstract
G-protein coupled receptors are key players mediating signal...
New limits of sensitivity of site-directed spin labeling electron paramagnetic resonance for membrane proteins #DNPNMR
From The DNP-NMR Blog:
New limits of sensitivity of site-directed spin labeling electron paramagnetic resonance for membrane proteins #DNPNMR
A nice overview how spinlabels can be used for structural biology studies. This includes pulsed EPR techniques such as PELDOR (DEER) and ODNP spectroscopy.
Bordignon, Enrica, and Stephanie Bleicken. “New Limits of Sensitivity of Site-Directed Spin Labeling Electron Paramagnetic Resonance for Membrane Proteins.” Biochimica et Biophysica Acta (BBA) - Biomembranes 1860, no. 4 (April 2018): 841–53. https://doi.org/10.1016/j.bbamem.2017.12.009.
[NMR paper] Biomolecular DNP-Supported NMR Spectroscopy using Site-Directed Spin Labeling.
Biomolecular DNP-Supported NMR Spectroscopy using Site-Directed Spin Labeling.
Related Articles Biomolecular DNP-Supported NMR Spectroscopy using Site-Directed Spin Labeling.
Chemistry. 2015 Sep 7;21(37):12971-7
Authors: van der Cruijsen EA, Koers EJ, Sauvée C, Hulse RE, Weingarth M, Ouari O, Perozo E, Tordo P, Baldus M
Abstract
Dynamic nuclear polarization (DNP) has been shown to greatly enhance spectroscopic sensitivity, creating novel opportunities for NMR studies on complex and large molecular assemblies in life and material...
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09-01-2015 10:48 AM
Biomolecular DNP-Supported NMR Spectroscopy using Site-Directed Spin Labeling
From The DNP-NMR Blog:
Biomolecular DNP-Supported NMR Spectroscopy using Site-Directed Spin Labeling
van der Cruijsen, E.A.W., et al., Biomolecular DNP-Supported NMR Spectroscopy using Site-Directed Spin Labeling. Chemistry – A European Journal, 2015: p. n/a-n/a.
http://dx.doi.org/10.1002/chem.201501376
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08-11-2015 02:50 AM
[NMR paper] Mapping Membrane Protein Backbone Dynamics: A Comparison of Site-Directed Spin Labeling with NMR (15)N-Relaxation Measurements.
Mapping Membrane Protein Backbone Dynamics: A Comparison of Site-Directed Spin Labeling with NMR (15)N-Relaxation Measurements.
Related Articles Mapping Membrane Protein Backbone Dynamics: A Comparison of Site-Directed Spin Labeling with NMR (15)N-Relaxation Measurements.
Biophys J. 2014 Oct 7;107(7):1697-1702
Authors: Lo RH, Kroncke BM, Solomon TL, Columbus L
Abstract
The ability to detect nanosecond backbone dynamics with site-directed spin labeling (SDSL) in soluble proteins has been well established. However, for membrane...
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10-09-2014 07:31 PM
Mapping Membrane Protein Backbone Dynamics: A Comparison of Site-Directed Spin Labeling with NMR 15N-Relaxation Measurements
Mapping Membrane Protein Backbone Dynamics: A Comparison of Site-Directed Spin Labeling with NMR 15N-Relaxation Measurements
Publication date: 7 October 2014
Source:Biophysical Journal, Volume 107, Issue 7</br>
Author(s): Ryan*H. Lo , Brett*M. Kroncke , Tsega*L. Solomon , Linda Columbus</br>
The ability to detect nanosecond backbone dynamics with site-directed spin labeling (SDSL) in soluble proteins has been well established. However, for membrane proteins, the nitroxide appears to have more interactions with the protein surface, potentially hindering the...