[NMR paper] Protein-Protein Interfaces Probed by Methyl-Labeling and Proton-Detected Solid-State NMR Spectroscopy.
Protein-Protein Interfaces Probed by Methyl-Labeling and Proton-Detected Solid-State NMR Spectroscopy.
Related Articles Protein-Protein Interfaces Probed by Methyl-Labeling and Proton-Detected Solid-State NMR Spectroscopy.
Chemphyschem. 2018 Jun 19;:
Authors: Zinke M, Fricke P, Lange S, Zinn-Justin S, Lange A
Abstract
Proton detection and fast magic-angle spinning have advanced biological solid-state NMR, allowing for the backbone assignment of complex protein assemblies with high sensitivity and resolution. However, so far no...
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06-20-2018 08:56 PM
[NMR paper] Direct Evidence of Imino Acid-Aromatic Interactions in Native Collagen Protein by DNP-Enhanced Solid-State NMR Spectroscopy.
Direct Evidence of Imino Acid-Aromatic Interactions in Native Collagen Protein by DNP-Enhanced Solid-State NMR Spectroscopy.
Related Articles Direct Evidence of Imino Acid-Aromatic Interactions in Native Collagen Protein by DNP-Enhanced Solid-State NMR Spectroscopy.
J Phys Chem Lett. 2014 Nov 20;5(22):4044-8
Authors: Singh C, Rai RK, Aussenac F, Sinha N
Abstract
Aromatic amino acids (AAAs) have rare presence (~1.4% abundance of Phe) inside of collagen protein, which is the most abundant animal protein playing a functional role in...
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Direct Evidence of Imino Acid–Aromatic Interactions in Native Collagen Protein by DNP-Enhanced Solid-State NMR Spectroscopy
From The DNP-NMR Blog:
Direct Evidence of Imino Acid–Aromatic Interactions in Native Collagen Protein by DNP-Enhanced Solid-State NMR Spectroscopy
Singh, C., et al., Direct Evidence of Imino Acid–Aromatic Interactions in Native Collagen Protein by DNP-Enhanced Solid-State NMR Spectroscopy. The Journal of Physical Chemistry Letters, 2014. 5(22): p. 4044-4048.
http://dx.doi.org/10.1021/jz502081j
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11-24-2014 04:15 PM
Structure Calculation from Unambiguous Long-Range Amide and Methyl (1)H-(1)H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy.
Structure Calculation from Unambiguous Long-Range Amide and Methyl (1)H-(1)H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy.
Structure Calculation from Unambiguous Long-Range Amide and Methyl (1)H-(1)H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy.
J Am Chem Soc. 2011 Mar 24;
Authors: Linser R, Bardiaux B, Higman V, Fink U, Reif B
Magic-angle spinning (MAS) solid-state NMR becomes an increasingly important tool for the determination of structures of membrane...
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03-26-2011 07:00 PM
Structure Calculation from Unambiguous Long-Range Amide and Methyl 1H-1H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy
Structure Calculation from Unambiguous Long-Range Amide and Methyl 1H-1H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy
Rasmus Linser, Benjamin Bardiaux, Victoria Higman, Uwe Fink and Bernd Reif
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja110222h/aop/images/medium/ja-2010-10222h_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja110222h
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/Dh0EBf8PwcY
Exploring Protein Structures by DNP-Enhanced Methyl Solid-State NMR Spectroscopy - ACS Publications
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