[NMR paper] Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach.
Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach.
Related Articles Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach.
J Biomol NMR. 2016 Jan 19;
Authors: Wang S, Matsuda I, Long F, Ishii Y
Abstract
This study demonstrates a novel spectral editing technique for protein solid-state NMR (SSNMR) to simplify the spectrum drastically and to reduce...
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01-20-2016 11:54 PM
Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach
Spectral editing at ultra-fast magic-angle-spinning in solid-state NMR: facilitating protein sequential signal assignment by HIGHLIGHT approach
Abstract
This study demonstrates a novel spectral editing technique for protein solid-state NMR (SSNMR) to simplify the spectrum drastically and to reduce the ambiguity for protein main-chain signal assignments in fast magic-angle-spinning (MAS) conditions at a wide frequency range of 40â??80Â*kHz. The approach termed HIGHLIGHT (Wang et al., in Chem Comm 51:15055â??15058, 2015) combines the reverse 13C,...
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01-19-2016 07:37 PM
[NMR paper] Proton detection for signal enhancement in solid-state NMR experiments on mobile species in membrane proteins.
Proton detection for signal enhancement in solid-state NMR experiments on mobile species in membrane proteins.
Related Articles Proton detection for signal enhancement in solid-state NMR experiments on mobile species in membrane proteins.
J Biomol NMR. 2015 Oct 22;
Authors: Ward ME, Ritz E, Ahmed MA, Bamm VV, Harauz G, Brown LS, Ladizhansky V
Abstract
Direct proton detection is becoming an increasingly popular method for enhancing sensitivity in solid-state nuclear magnetic resonance spectroscopy. Generally, these experiments...
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10-24-2015 06:43 PM
Proton detection for signal enhancement in solid-state NMR experiments on mobile species in membrane proteins
Proton detection for signal enhancement in solid-state NMR experiments on mobile species in membrane proteins
Abstract
Direct proton detection is becoming an increasingly popular method for enhancing sensitivity in solid-state nuclear magnetic resonance spectroscopy. Generally, these experiments require extensive deuteration of the protein, fast magic angle spinning (MAS), or a combination of both. Here, we implement direct proton detection to selectively observe the mobile entities in fully-protonated membrane proteins at moderate MAS frequencies. We...
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10-23-2015 02:14 PM
[NMR paper] Advanced Solid-State NMR Approaches for Structure Determination of Membrane Proteins and Amyloid Fibrils.
Advanced Solid-State NMR Approaches for Structure Determination of Membrane Proteins and Amyloid Fibrils.
Advanced Solid-State NMR Approaches for Structure Determination of Membrane Proteins and Amyloid Fibrils.
Acc Chem Res. 2013 May 10;
Authors: Tang M, Comellas G, Rienstra CM
Abstract
Solid-state NMR (SSNMR) spectroscopy has become an important technique for studying the biophysics and structure biology of proteins. This technique is especially useful for insoluble membrane proteins and amyloid fibrils, which are essential for...
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05-11-2013 10:26 PM
[NMR paper] Protein Structure Determination by Magic-Angle Spinning Solid-State NMR, and Insights into the Formation, Structure, and Stability of Amyloid Fibrils.
Protein Structure Determination by Magic-Angle Spinning Solid-State NMR, and Insights into the Formation, Structure, and Stability of Amyloid Fibrils.
Related Articles Protein Structure Determination by Magic-Angle Spinning Solid-State NMR, and Insights into the Formation, Structure, and Stability of Amyloid Fibrils.
Annu Rev Biophys. 2013 Mar 22;
Authors: Comellas G, Rienstra CM
Abstract
Protein structure determination methods using magic-angle spinning solidstate nuclear magnetic resonance (MAS SSNMR) have experienced a remarkable...
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03-27-2013 03:33 PM
[NMR paper] Proteolytic E-cadherin activation followed by solution NMR and X-ray crystallography.
Proteolytic E-cadherin activation followed by solution NMR and X-ray crystallography.
Related Articles Proteolytic E-cadherin activation followed by solution NMR and X-ray crystallography.
EMBO J. 2004 Apr 21;23(8):1699-708
Authors: Häussinger D, Ahrens T, Aberle T, Engel J, Stetefeld J, Grzesiek S
Cellular adhesion by classical cadherins depends critically on the exact proteolytic removal of their N-terminal prosequences. In this combined solution NMR and X-ray crystallographic study, the consequences of propeptide cleavage of an epithelial...
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11-24-2010 09:51 PM
[Question from NMRWiki Q&A forum] Examples of protein degradation eg HSQC?
Examples of protein degradation eg HSQC?
Anyone know any websites or papers that show protein degradation in an HSQC for example? I wanted to know what to look for in old samples when I have them. Either that, or could someone put one up on the wiki for me to look at?
Check if somebody has answered this question on NMRWiki QA forum
Epigallocatechin Gallate Remodels Fibrils of LatticeCorneal Dystrophy Protein, Facilitating Proteolytic Degradation andPreventing Formation of Membrane-Permeabilizing Species
Linear Mode
