Dietary fiber like konjac glucomannan (KGM) is important in maintaining good human health. There is no established method for quantifying the average degree of acetylation DA of this polysaccharide. Polysaccharides are notoriously difficult to dissolve. In this study, KGM could not be fully dissolved in common solvents and was characterized in the solid state. ATR-FTIR spectroscopy enabled a fast qualitative assessment of acetylation, selective to the outer layer of KGM particles, and...
[NMR paper] Selective detection of protein acetylation by NMR spectroscopy
Selective detection of protein acetylation by NMR spectroscopy
Selective detection of biomolecules and their modifications in cells is essential for understanding cell functions and diseases. We have developed an NMR pulse sequence, Ac-FIND (Acetylation-FIltered aNd eDited), which uses isotope editing/filtering techniques for selective detection of protein acetylation. Acetylation of the N-terminus and lysine side chains by N-succinimidyl acetate was selectively observed for intrinsically disordered ?-synuclein and well-ordered ubiquitin. Furthermore, when...
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[NMR paper] Assessing Interactions Between a Polytopic Membrane Protein and Lipid Bilayers Using Differential Scanning Calorimetry and Solid-State NMR.
Assessing Interactions Between a Polytopic Membrane Protein and Lipid Bilayers Using Differential Scanning Calorimetry and Solid-State NMR.
Related Articles Assessing Interactions Between a Polytopic Membrane Protein and Lipid Bilayers Using Differential Scanning Calorimetry and Solid-State NMR.
J Phys Chem B. 2018 Feb 19;:
Authors: Banigan JR, Leninger M, Her AS, Traaseth NJ
Abstract
It is known that the lipid composition within a cellular membrane can influence membrane protein structure and function. In this Article, we...
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[NMR paper] Quantification of protein secondary structure by (13)C solid-state NMR.
Quantification of protein secondary structure by (13)C solid-state NMR.
Related Articles Quantification of protein secondary structure by (13)C solid-state NMR.
Anal Bioanal Chem. 2016 Apr 11;
Authors: Andrade FD, Forato LA, Bernardes Filho R, Colnago LA
Abstract
High-resolution (13)C solid-state NMR stands out as one of the most promising techniques to solve the structure of insoluble proteins featuring biological and technological importance. The simplest nuclear magnetic resonance (NMR) spectroscopy method to quantify the...
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Solid-State NMR and FTIR Study of a Neuronal Calcium Sensor (NCS) Protein, Recoverin
Solid-State NMR and FTIR Study of a Neuronal Calcium Sensor (NCS) Protein, Recoverin
Publication date: 28 January 2014
Source:Biophysical Journal, Volume 106, Issue 2, Supplement 1</br>
Author(s): Kim Potvin-Fournier , Audrey Picard-Lafond , Melanie Schneider , Geneviève Valois-Paillard , Thierry Lefèvre , Philippe Calvez , Line Cantin , Christian Salesse , Michèle Auger</br>
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01-29-2014 12:50 AM
[NMR paper] Determining the mode of action involved in the antimicrobial activity of synthetic peptides: a solid-state NMR and FTIR study.
Determining the mode of action involved in the antimicrobial activity of synthetic peptides: a solid-state NMR and FTIR study.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles Determining the mode of action involved in the antimicrobial activity of synthetic peptides: a solid-state NMR and FTIR study.
Biophys J. 2012 Oct 3;103(7):1470-9
Authors: Lorin A, Noël M, Provencher MÈ, Turcotte V, Cardinal S, Lagüe P, Voyer N, Auger M
Abstract
We have previously...
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[NMR paper] Membrane insertion of a lipidated ras peptide studied by FTIR, solid-state NMR, and n
Membrane insertion of a lipidated ras peptide studied by FTIR, solid-state NMR, and neutron diffraction spectroscopy.
Related Articles Membrane insertion of a lipidated ras peptide studied by FTIR, solid-state NMR, and neutron diffraction spectroscopy.
J Am Chem Soc. 2003 Apr 9;125(14):4070-9
Authors: Huster D, Vogel A, Katzka C, Scheidt HA, Binder H, Dante S, Gutberlet T, Zschörnig O, Waldmann H, Arnold K
Membrane binding of a doubly lipid modified heptapeptide from the C-terminus of the human N-ras protein was studied by Fourier transform...
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11-24-2010 09:01 PM
Quantification of protein backbone hydrogen-deuterium exchange rates by solid state N
Quantification of protein backbone hydrogen-deuterium exchange rates by solid state NMR spectroscopy
Abstract We present the quantification of backbone amide hydrogen-deuterium exchange rates (HDX) for immobilized proteins. The experiments make use of the deuterium isotope effect on the amide nitrogen chemical shift, as well as on proton dilution by deuteration. We find that backbone amides in the microcrystalline α-spectrin SH3 domain exchange rather slowly with the solvent (with exchange rates negligible within the individual 15Nâ??T 1 timescales). We observed chemical exchange for 6...
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Quantification of protein backbone hydrogen-deuterium exchange rates by solid state N
Quantification of protein backbone hydrogen-deuterium exchange rates by solid state NMR spectroscopy.
Related Articles Quantification of protein backbone hydrogen-deuterium exchange rates by solid state NMR spectroscopy.
J Biomol NMR. 2010 Oct 20;
Authors: Del Amo JM, Fink U, Reif B
We present the quantification of backbone amide hydrogen-deuterium exchange rates (HDX) for immobilized proteins. The experiments make use of the deuterium isotope effect on the amide nitrogen chemical shift, as well as on proton dilution by deuteration. We find that...
Assessing the quantification of acetylation in konjac glucomannan via ATR-FTIR and solid-state NMR spectroscopy
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