Progress in NMR in general and in biomolecular applications in particular is driven by increasing magnetic-field strengths leading to improved resolution and sensitivity of the NMR spectra. Recently, persistent superconducting magnets at a magnetic field strength (magnetic induction) of 28.2 T corresponding to 1200Â*MHz proton resonance frequency became commercially available. We present here a collection of high-field NMR spectra of a variety of proteins, including molecular machines, membrane proteins, viral capsids, fibrils and large molecular assemblies. We show this large panel in order to provide an overview over a range of representative systems under study, rather than a single best performing model system. We discuss both carbon-13 and proton-detected experiments, and show that in 13C spectra substantially higher numbers of peaks can be resolved compared to 850Â*MHz while for 1H spectra the most impressive increase in resolution is observed for aliphatic side-chain resonances.
[NMR paper] Biomolecular complex viewed by dynamic nuclear polarization solid-state NMR spectroscopy.
Biomolecular complex viewed by dynamic nuclear polarization solid-state NMR spectroscopy.
Related Articles Biomolecular complex viewed by dynamic nuclear polarization solid-state NMR spectroscopy.
Biochem Soc Trans. 2020 May 07;:
Authors: Chakraborty A, Deligey F, Quach J, Mentink-Vigier F, Wang P, Wang T
Abstract
Solid-state nuclear magnetic resonance (ssNMR) is an indispensable tool for elucidating the structure and dynamics of insoluble and non-crystalline biomolecules. The recent advances in the sensitivity-enhancing...
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05-08-2020 06:11 PM
[NMR paper] Recent Advances in High-Resolution Solid-State NMR Spectroscopy.
Recent Advances in High-Resolution Solid-State NMR Spectroscopy.
Related Articles Recent Advances in High-Resolution Solid-State NMR Spectroscopy.
Angew Chem Int Ed Engl. 2001 Jun 01;40(11):2045-2050
Authors: Schwalbe H, Bielecki A
Abstract
Diverse complex systems may be studied by the new methods in solid-state NMR spectroscopy described herein. These methods use magic-angle spinning (MAS) on samples in oriented bilayers (right picture) and in orientationally disordered samples (left picture). Systems as diverse as uniformly 13...
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05-03-2018 06:46 PM
[NMR paper] Covariance spectroscopy in high-resolution multi-dimensional solid-state NMR.
Covariance spectroscopy in high-resolution multi-dimensional solid-state NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Covariance spectroscopy in high-resolution multi-dimensional solid-state NMR.
J Magn Reson. 2014 Feb;239:57-60
Authors: Lin EC, Opella SJ
Abstract
Covariance spectroscopy (COV), a statistical method that provides increased sensitivity, can be applied to two-dimensional high-resolution solid-state NMR...
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10-07-2014 02:31 PM
Fractional deuteration applied to biomolecular solid-state NMR spectroscopy
Fractional deuteration applied to biomolecular solid-state NMR spectroscopy
Abstract Solid-state Nuclear Magnetic Resonance can provide detailed insight into structural and dynamical aspects of complex biomolecules. With increasing molecular size, advanced approaches for spectral simplification and the detection of medium to long-range contacts become of critical relevance. We have analyzed the protonation pattern of a membrane-embedded ion channel that was obtained from bacterial expression using protonated precursors and D2O medium. We find an overall reduction of 50% in protein...
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11-24-2011 12:25 AM
Straightforward, effective calibration of SPINAL-64 decoupling results in the enhancement of sensitivity and resolution of biomolecular solid-state NMR.
Straightforward, effective calibration of SPINAL-64 decoupling results in the enhancement of sensitivity and resolution of biomolecular solid-state NMR.
Straightforward, effective calibration of SPINAL-64 decoupling results in the enhancement of sensitivity and resolution of biomolecular solid-state NMR.
J Magn Reson. 2010 Dec 31;
Authors: Comellas G, Lopez JJ, Nieuwkoop AJ, Lemkau LR, Rienstra CM
We describe a simple yet highly effective optimization strategy for SPINAL-64 (1)H decoupling conditions for magic-angle spinning solid-state NMR. With...
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02-08-2011 06:28 PM
Straightforward, effective calibration of SPINAL-64 decoupling results in the enhancement of sensitivity and resolution of biomolecular solid-state NMR
Straightforward, effective calibration of SPINAL-64 decoupling results in the enhancement of sensitivity and resolution of biomolecular solid-state NMR
Publication year: 2010
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 31 December 2010</br>
Gemma, Comellas , Jakob J., Lopez , Andrew J., Nieuwkoop , Luisel R., Lemkau , Chad M., Rienstra</br>
We describe a simple yet highly effective optimization strategy for SPINAL-64 1H decoupling conditions for magic-angle spinning solid-state NMR. With adjustment of the phase angles in a coupled manner,...
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01-01-2011 08:57 AM
[NMR paper] Resolution enhancement in multidimensional solid-state NMR spectroscopy of proteins u
Resolution enhancement in multidimensional solid-state NMR spectroscopy of proteins using spin-state selection.
Related Articles Resolution enhancement in multidimensional solid-state NMR spectroscopy of proteins using spin-state selection.
J Am Chem Soc. 2003 Oct 1;125(39):11816-7
Authors: Duma L, Hediger S, Brutscher B, Böckmann A, Emsley L
We show that the resolution of homonuclear multidimensional solid-state NMR correlation experiments can be significantly improved using transition selection and spin-state-selective polarization transfer...
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11-24-2010 09:16 PM
[NMR paper] Three-dimensional solid-state NMR spectroscopy is essential for resolution of resonan
Three-dimensional solid-state NMR spectroscopy is essential for resolution of resonances from in-plane residues in uniformly (15)N-labeled helical membrane proteins in oriented lipid bilayers.
Related Articles Three-dimensional solid-state NMR spectroscopy is essential for resolution of resonances from in-plane residues in uniformly (15)N-labeled helical membrane proteins in oriented lipid bilayers.
J Magn Reson. 2000 May;144(1):156-61
Authors: Marassi FM, Ma C, Gesell JJ, Opella SJ
Uniformly (15)N-labeled samples of membrane proteins with...
Biomolecular solid-state NMR spectroscopy at 1200Â*MHz: the gain in resolution
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