[NMR paper] Sedimentation of large, soluble proteins up to 140 kDa for (1)H-detected MAS NMR and (13)C DNP NMR - practical aspects
Sedimentation of large, soluble proteins up to 140 kDa for (1)H-detected MAS NMR and (13)C DNP NMR - practical aspects
Solution NMR is typically applied to biological systems with molecular weights < 40 kDa whereas magic-angle-spinning (MAS) solid-state NMR traditionally targets very large, oligomeric proteins and complexes exceeding 500 kDa in mass, including fibrils and crystalline protein preparations. Here, we propose that the gap between these size regimes can be filled by the approach presented that enables investigation of large, soluble and fully protonated proteins in the range of...
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06-21-2024 10:12 PM
[NMR paper] Sedimentation of large, soluble proteins up to 140 kDa for 1H-detected MAS NMR and 13C DNP NMR - practical aspects
Sedimentation of large, soluble proteins up to 140 kDa for 1H-detected MAS NMR and 13C DNP NMR - practical aspects
Solution NMR is typically applied to biological systems with molecular weights < 40 kDa whereas magic-angle-spinning (MAS) solid-state NMR traditionally targets very large, oligomeric proteins and complexes exceeding 500 kDa in mass, including fibrils and crystalline protein preparations. Here, we propose that the gap between these size regimes can be filled by the approach presented that enables investigation of large, soluble and fully protonated proteins in the range of...
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03-11-2024 10:30 PM
Immobilization of soluble protein complexes in MAS solid-state NMR: Sedimentation versus viscosity
From The DNP-NMR Blog:
Immobilization of soluble protein complexes in MAS solid-state NMR: Sedimentation versus viscosity
Sarkar, R., et al., Immobilization of soluble protein complexes in MAS solid-state NMR: Sedimentation versus viscosity. Solid State Nucl Magn Reson, 2016. 76-77: p. 7-14.
http://www.ncbi.nlm.nih.gov/pubmed/27017576
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07-22-2016 02:21 PM
[NMR paper] Immobilization of soluble protein complexes in MAS solid-state NMR: Sedimentation versus viscosity.
Immobilization of soluble protein complexes in MAS solid-state NMR: Sedimentation versus viscosity.
Related Articles Immobilization of soluble protein complexes in MAS solid-state NMR: Sedimentation versus viscosity.
Solid State Nucl Magn Reson. 2016 Mar 15;76-77:7-14
Authors: Sarkar R, Mainz A, Busi B, Barbet-Massin E, Kranz M, Hofmann T, Reif B
Abstract
In recent years, MAS solid-state NMR has emerged as a technique for the investigation of soluble protein complexes. It was found that high molecular weight complexes do not need...
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03-29-2016 01:43 AM
Immobilization of soluble protein complexes in MAS solid-state NMR: Sedimentation versus viscosity
Immobilization of soluble protein complexes in MAS solid-state NMR: Sedimentation versus viscosity
Publication date: Available online 15 March 2016
Source:Solid State Nuclear Magnetic Resonance</br>
Author(s): Riddhiman Sarkar, Andi Mainz, Baptiste Busi, Emeline Barbet-Massin, Maximilian Kranz, Thomas Hofmann, Bernd Reif</br>
In recent years, MAS solid-state NMR has emerged as a technique for the investigation of soluble protein complexes. It was found that high molecular weight complexes do not need to be crystallized in order to obtain an immobilized...
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03-16-2016 12:13 AM
TROSY NMR Spectroscopy of Large Soluble Proteins.
TROSY NMR Spectroscopy of Large Soluble Proteins.
TROSY NMR Spectroscopy of Large Soluble Proteins.
Top Curr Chem. 2011 Sep 17;
Authors: Xu Y, Matthews S
Abstract
Solution nuclear magnetic resonance spectroscopy is usually only used to study proteins with molecular weight not exceeding about 50 kDa. This size limit has been lifted significantly in recent years, thanks to the development of labelling methods and the application of transverse-relaxation optimized spectroscopy (TROSY). In particular, methyl-specific labelling and...
Sedimentation of large, soluble proteins up t o 140?kDa for - ResearchGate
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