Protein Analysis by (31)P NMR Spectroscopy in Ionic Liquid: Quantitative Determination of Enzymatically Created Cross-Links.
Protein Analysis by (31)P NMR Spectroscopy in Ionic Liquid: Quantitative Determination of Enzymatically Created Cross-Links.
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...
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[NMR paper] Microsecond timescale backbone conformational dynamics in ubiquitin studied with NMR
Microsecond timescale backbone conformational dynamics in ubiquitin studied with NMR R1rho relaxation experiments.
Related Articles Microsecond timescale backbone conformational dynamics in ubiquitin studied with NMR R1rho relaxation experiments.
Protein Sci. 2005 Mar;14(3):735-42
Authors: Massi F, Grey MJ, Palmer AG
NMR spin relaxation experiments are used to characterize the dynamics of the backbone of ubiquitin. Chemical exchange processes affecting residues Ile 23, Asn 25, Thr 55, and Val 70 are characterized using on- and off-resonance...
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11-24-2010 11:14 PM
[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.
Related Articles Addressing the overlap problem in the quantitative analysis of two dimensional NMR spectra: application to (15)N relaxation measurements.
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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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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10-29-2010 07:05 PM
[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.
Related Articles Quantitative analysis of 1H NMR detected proteins in the rat cerebral cortex in vivo and in vitro.
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...
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[NMR paper] 3 Nsec molecular dynamics simulation of the protein ubiquitin and comparison with X-r
3 Nsec molecular dynamics simulation of the protein ubiquitin and comparison with X-ray crystal and solution NMR structures.
Related Articles 3 Nsec molecular dynamics simulation of the protein ubiquitin and comparison with X-ray crystal and solution NMR structures.
J Biomol Struct Dyn. 1992 Apr;9(5):935-49
Authors: Braatz JA, Paulsen MD, Ornstein RL
Mainly due to computational limitations, past protein molecular dynamics simulations have rarely been extended to 300 psec; we are not aware of any published results beyond 350 psec. The present...
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[NMR paper] Analysis of the backbone dynamics of interleukin-1 beta using two-dimensional inverse
Analysis of the backbone dynamics of interleukin-1 beta using two-dimensional inverse detected heteronuclear 15N-1H NMR spectroscopy.
Related Articles Analysis of the backbone dynamics of interleukin-1 beta using two-dimensional inverse detected heteronuclear 15N-1H NMR spectroscopy.
Biochemistry. 1990 Aug 14;29(32):7387-401
Authors: Clore GM, Driscoll PC, Wingfield PT, Gronenborn AM
The backbone dynamics of uniformly 15N-labeled interleukin-1 beta are investigated by using two-dimensional inverse detected heteronuclear 15N-1H NMR...
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[NMR paper] An NMR analysis of the reaction of ubiquitin with [acetyl-1-13C]aspirin.
An NMR analysis of the reaction of ubiquitin with aspirin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles An NMR analysis of the reaction of ubiquitin with aspirin.
Biochem Pharmacol. 1999 Jun 1;57(11):1233-44
Authors: Macdonald JM, LeBlanc DA, Haas AL, London RE
The acetylation of ubiquitin by aspirin has been studied using 2D NMR methods. Studies performed in a 50:50 H2O:D2O medium show doubling of the acetyl carbonyl resonances, indicating that all of the stable...
Quantitative Analysis of Protein Backbone Dynamics in Microcrystalline Ubiquitin by S
Linear Mode
