Related ArticlesHigh-sensitivity protein solid-state NMR spectroscopy.
Curr Opin Struct Biol. 2019 Apr 25;:
Authors: Mandala VS, Hong M
Abstract
The sensitivity of solid-state nuclear magnetic resonance (SSNMR) spectroscopy for structural biology is significantly increased by 1H detection under fast magic-angle spinning (MAS) and by dynamic nuclear polarization (DNP) from electron spins to nuclear spins. The former allows studies of the structure and dynamics of small quantities of proteins under physiological conditions, while the latter permits studies of large biomolecular complexes in lipid membranes and cells, protein intermediates, and protein conformational distributions. We highlight recent applications of these two emerging SSNMR technologies and point out areas for future development.
PMID: 31031067 [PubMed - as supplied by publisher]
[NMR paper] High-Sensitivity Rheo-NMR Spectroscopy for Protein Studies.
High-Sensitivity Rheo-NMR Spectroscopy for Protein Studies.
High-Sensitivity Rheo-NMR Spectroscopy for Protein Studies.
Anal Chem. 2017 Jun 30;:
Authors: Morimoto D, Walinda E, Iwakawa N, Nishizawa M, Kawata Y, Yamamoto A, Shirakawa M, Scheler U, Sugase K
Abstract
Shear stress can induce structural deformation of proteins, which might result in aggregate formation. Rheo-NMR spectroscopy has the potential to monitor structural changes in proteins under shear stress at the atomic level; however, existing Rheo-NMR methodologies...
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07-01-2017 11:41 AM
[NMR paper] A Novel High-Resolution and Sensitivity-Enhanced Three-Dimensional Solid-State NMR Experiment Under Ultrafast Magic Angle Spinning Conditions.
A Novel High-Resolution and Sensitivity-Enhanced Three-Dimensional Solid-State NMR Experiment Under Ultrafast Magic Angle Spinning Conditions.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_npg.gif http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles A Novel High-Resolution and Sensitivity-Enhanced Three-Dimensional Solid-State NMR Experiment Under Ultrafast Magic Angle Spinning Conditions.
Sci Rep. 2015;5:11810
...
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08-03-2016 04:58 AM
[NMR paper] Correlating Lipid Bilayer Fluidity with Sensitivity and Resolution of Polytopic Membrane Protein Spectra by Solid-State NMR Spectroscopy.
Correlating Lipid Bilayer Fluidity with Sensitivity and Resolution of Polytopic Membrane Protein Spectra by Solid-State NMR Spectroscopy.
Related Articles Correlating Lipid Bilayer Fluidity with Sensitivity and Resolution of Polytopic Membrane Protein Spectra by Solid-State NMR Spectroscopy.
Biochim Biophys Acta. 2014 May 13;
Authors: Banigan JR, Gayen A, Traaseth NJ
Abstract
Solid-state NMR spectroscopy has emerged as an excellent tool to study the structure and dynamics of membrane proteins under native-like conditions in lipid...
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05-20-2014 11:10 PM
Correlating Lipid Bilayer Fluidity with Sensitivity and Resolution of Polytopic Membrane Protein Spectra by Solid-State NMR Spectroscopy
Correlating Lipid Bilayer Fluidity with Sensitivity and Resolution of Polytopic Membrane Protein Spectra by Solid-State NMR Spectroscopy
Publication date: Available online 13 May 2014
Source:Biochimica et Biophysica Acta (BBA) - Biomembranes</br>
Author(s): James R. Banigan , Anindita Gayen , Nathaniel J. Traaseth</br>
Solid-state NMR spectroscopy has emerged as an excellent tool to study the structure and dynamics of membrane proteins under native-like conditions in lipid bilayers. One of the key considerations in experimental design is the uniaxial rotational...
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05-14-2014 04:50 AM
[NMR paper] High-resolution solid-state NMR spectroscopy of the prion protein HET-s in its amyloi
High-resolution solid-state NMR spectroscopy of the prion protein HET-s in its amyloid conformation.
Related Articles High-resolution solid-state NMR spectroscopy of the prion protein HET-s in its amyloid conformation.
Angew Chem Int Ed Engl. 2005 Apr 15;44(16):2441-4
Authors: Siemer AB, Ritter C, Ernst M, Riek R, Meier BH
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11-25-2010 08:21 PM
[NMR paper] Sensitivity enhancement in two-dimensional solid-state NMR spectroscopy by transverse
Sensitivity enhancement in two-dimensional solid-state NMR spectroscopy by transverse mixing.
Related Articles Sensitivity enhancement in two-dimensional solid-state NMR spectroscopy by transverse mixing.
Chemphyschem. 2004 Jun 21;5(6):863-8
Authors: Tycko R
The sensitivity of two-dimensional (2D) 13C-13C solid-state NMR spectroscopy under magic-angle spinning (MAS) is shown to be enhanced by the use of transverse polarization transfer in place of the conventional longitudinal polarization transfer. Experimental results are reported for 2D...
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11-24-2010 09:51 PM
High resolution 13C-detected solid-state NMR spectroscopy of a deuterated protein
High resolution 13C-detected solid-state NMR spectroscopy of a deuterated protein
Abstract High resolution 13C-detected solid-state NMR spectra of the deuterated beta-1 immunoglobulin binding domain of the protein G (GB1) have been collected to show that all 15N, 13Cā?², 13CĪ± and 13CĪ² sites are resolved in 13Cā??13C and 15Nā??13C spectra, with significant improvement in T 2 relaxation times and resolution at high magnetic field (750 MHz). The comparison of echo T 2 values between deuterated and protonated GB1 at various spinning rates and under different decoupling schemes indicates...
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High resolution (13)C-detected solid-state NMR spectroscopy of a deuterated protein.
High resolution (13)C-detected solid-state NMR spectroscopy of a deuterated protein.
Related Articles High resolution (13)C-detected solid-state NMR spectroscopy of a deuterated protein.
J Biomol NMR. 2010 Aug 29;
Authors: Tang M, Comellas G, Mueller LJ, Rienstra CM
High resolution (13)C-detected solid-state NMR spectra of the deuterated beta-1 immunoglobulin binding domain of the protein G (GB1) have been collected to show that all (15)N, (13)C', (13)Calpha and (13)Cbeta sites are resolved in (13)C-(13)C and (15)N-(13)C spectra, with significant...
High-sensitivity protein solid-state NMR spectroscopy.
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