Protein Analysis by (31)P NMR Spectroscopy in Ionic Liquid: Quantitative Determination of Enzymatically Created Cross-Links.
J Agric Food Chem. 2011 Jan 10;
Authors: Monogioudi E, Permi P, Filpponen I, Lienemann M, Li B, Argyropoulos D, Buchert J, Mattinen ML
Cross-linking of ?-casein by Trichoderma reesei tyrosinase (TrTyr) and Streptoverticillium mobaraense transglutaminase (Tgase) was analyzed by (31)P nuclear magnetic resonance (NMR) spectroscopy in ionic liquid (IL). According to (31)P NMR, 91% of the tyrosine side chains were cross-linked by TrTyr at high dosages. When Tgase was used, no changes were observed because a different cross-linking mechanism was operational. However, this verified the success of the phosphitylation of phenolics within the protein matrix in the IL. Atomic force microscopy (AFM) in solid state showed that disk-shaped nanoparticles were formed in the reactions with average diameters of 80 and 20 nm for TrTyr and Tgase, respectively. These data further advance the current understanding of the action of tyrosinases on proteins on molecular and chemical bond levels. Quantitative (31)P NMR in IL was shown to be a simple and efficient method for the study of protein modification.
PMID: 21218836 [PubMed - as supplied by publisher]
A rigid disulfide-linked nitroxide side chain simplifies the quantitative analysis of PRE data
A rigid disulfide-linked nitroxide side chain simplifies the quantitative analysis of PRE data
Abstract The measurement of 1H transverse paramagnetic relaxation enhancement (PRE) has been used in biomolecular systems to determine long-range distance restraints and to visualize sparsely-populated transient states. The intrinsic flexibility of most nitroxide and metal-chelating paramagnetic spin-labels, however, complicates the quantitative interpretation of PREs due to delocalization of the paramagnetic center. Here, we present a novel, disulfide-linked nitroxide spin label, R1p, as...
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[NMR paper] Addressing the overlap problem in the quantitative analysis of two dimensional NMR sp
Addressing the overlap problem in the quantitative analysis of two dimensional NMR spectra: application to (15)N relaxation measurements.
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J Biomol NMR. 2004 Nov;30(3):347-52
Authors: Tugarinov V, Choy WY, Kupce E, Kay LE
A quantitative analysis of 2D (1)H-(15)N spectra is often complicated by resonance overlap. Here a simple method is presented for resolving overlapped correlations by...
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[NMR paper] Automated NMR determination of protein backbone dihedral angles from cross-correlated
Automated NMR determination of protein backbone dihedral angles from cross-correlated spin relaxation.
Related Articles Automated NMR determination of protein backbone dihedral angles from cross-correlated spin relaxation.
J Biomol NMR. 2002 Apr;22(4):349-63
Authors: Kloiber K, Schüler W, Konrat R
The simultaneous interpretation of a suite of dipole-dipole and dipole-CSA cross-correlation rates involving the backbone nuclei 13Calpha, 1Halpha, 13CO, 15N and 1HN can be used to resolve the ambiguities associated with each individual...
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Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by S
Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by Solid-State NMR Spectroscopy.
Related Articles Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by Solid-State NMR Spectroscopy.
J Am Chem Soc. 2010 Oct 26;
Authors: Schanda P, Meier BH, Ernst M
Characterization of protein dynamics by solid-state NMR spectroscopy requires robust and accurate measurement protocols, which are not yet fully developed. In this study, we investigate the backbone dynamics of microcrystalline ubiquitin...
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Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by S
Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by Solid-State NMR Spectroscopy
Paul Schanda, Beat H. Meier and Matthias Ernst
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja100726a/aop/images/medium/ja-2010-00726a_0001.gif
Journal of the American Chemical Society
DOI: 10.1021/ja100726a
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http://feeds.feedburner.com/~r/acs/jacsat/~4/vMvBmzNs148
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Plant Cell-Wall Cross-Links by REDOR NMR Spectroscopy.
Plant Cell-Wall Cross-Links by REDOR NMR Spectroscopy.
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J Am Chem Soc. 2010 Oct 21;
Authors: Cegelski L, O'Connor RD, Stueber D, Singh M, Poliks B, Schaefer J
We present a new method that integrates selective biosynthetic labeling and solid-state NMR detection to identify in situ important protein cross-links in plant cell walls. We have labeled soybean cells by growth in media containing l-tyrosine and l-tyrosine, compared whole-cell and cell-wall (13)C CPMAS spectra, and...
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Plant Cell-Wall Cross-Links by REDOR NMR Spectroscopy
Plant Cell-Wall Cross-Links by REDOR NMR Spectroscopy
Lynette Cegelski, Robert D. O’Connor, Dirk Stueber, Manmilan Singh, Barbara Poliks and Jacob Schaefer
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja104827k/aop/images/medium/ja-2010-04827k_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja104827k
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http://feeds.feedburner.com/~r/acs/jacsat/~4/1kI0vIFK7eU
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[NMR paper] Quantitative analysis of 1H NMR detected proteins in the rat cerebral cortex in vivo
Quantitative analysis of 1H NMR detected proteins in the rat cerebral cortex in vivo and in vitro.
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NMR Biomed. 1993 Jul-Aug;6(4):242-7
Authors: Kauppinen RA, Niskanen T, Hakumäki J, Williams SR
Spectral editing experiments were used to quantify CH3 groups from macromolecular species in the chemical shift region from 1.2 to 1.4 ppm of rat cerebrum in vivo. Two peaks centred at 1.22 and 1.40 ppm were revealed when irradiation was...
Protein Analysis by (31)P NMR Spectroscopy in Ionic Liquid: Quantitative Determination of Enzymatically Created Cross-Links.
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