[NMR paper] Effect of Substitution Degree and Homogeneity on Cyclodextrin-Ligand Complex Stability: Comparison of Fenbufen and Fenoprofen Using CD and NMR Spectroscopy
Effect of Substitution Degree and Homogeneity on Cyclodextrin-Ligand Complex Stability: Comparison of Fenbufen and Fenoprofen Using CD and NMR Spectroscopy
The stability of host-guest complexes of two NSAID drugs with similar physicochemical properties, fenbufen and fenoprofen, was investigated by comparing induced circular dichroism and ¹H nuclear magnetic resonance methods using eight cyclodextrins of different degrees of substitution and isomeric purity as guest compounds. These cyclodextrins include native ?-cyclodextrin (BCyD), 2,6-dimethyl-?-cyclodextrin 50 (DIMEB50), 80 (DIMEB80) and 95% (DIMEB95) isomerically pure versions, low-methylated...
[NMR paper] Determination of modification degree of polysialylated therapeutic proteins using (1)H-NMR spectroscopy
Determination of modification degree of polysialylated therapeutic proteins using (1)H-NMR spectroscopy
Water soluble polymers and their derivatives bound to proteins can dramatically favor the biological activity of new drugs and vaccines. Quantification of the modification degree of the protein is crucial during the development and licensing phase and later in order to monitor the industrial production process and to match product specification. In this work, we describe an innovative way to measure directly the modification degree of polysialylated proteins using proton NMR (Nuclear...
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07-03-2021 08:12 PM
Improving B1 field homogeneity in dielectric tube resonators for EPR spectroscopy via controlled shaping of the dielectric insert
From The DNP-NMR Blog:
Improving B1 field homogeneity in dielectric tube resonators for EPR spectroscopy via controlled shaping of the dielectric insert
Syryamina, Victoria N., Anna G. Matveeva, Yan V. Vasiliev, Anton Savitsky, and Yuri A. Grishin. “Improving B1 Field Homogeneity in Dielectric Tube Resonators for EPR Spectroscopy via Controlled Shaping of the Dielectric Insert.” Journal of Magnetic Resonance 311 (February 2020): 106685.
https://doi.org/10.1016/j.jmr.2020.106685.
We propose an approach for improving the homogeneity of microwave magnetic field amplitude in a...
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03-16-2020 04:59 PM
Systematic Identification of Protein–Metabolite Interactions in Complex MetaboliteMixtures by Ligand-Detected Nuclear Magnetic Resonance Spectroscopy
Systematic Identification of Protein–Metabolite Interactions in Complex MetaboliteMixtures by Ligand-Detected Nuclear Magnetic Resonance Spectroscopy
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b01291/20160425/images/medium/bi-2015-012916_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b01291
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/TQ5IVPOPNRw
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04-26-2016 12:14 PM
[NMR paper] Systematic identification of protein-metabolite interactions in complex metabolite mixtures by ligand-detected NMR spectroscopy.
Systematic identification of protein-metabolite interactions in complex metabolite mixtures by ligand-detected NMR spectroscopy.
Systematic identification of protein-metabolite interactions in complex metabolite mixtures by ligand-detected NMR spectroscopy.
Biochemistry. 2016 Apr 11;
Authors: Nikolaev YV, Kochanowski K, Link H, Sauer U, Allain FH
Abstract
Protein-metabolite interactions play a vital role in the regulation of numerous cellular processes. Consequently, identifying such interactions is a key prerequisite for...
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04-12-2016 09:12 PM
[NMR paper] Differences in heat stability and ligand binding among ?-lactoglobulin genetic variants A, B and C using (1)H NMR and fluorescence quenching.
Differences in heat stability and ligand binding among ?-lactoglobulin genetic variants A, B and C using (1)H NMR and fluorescence quenching.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Differences in heat stability and ligand binding among ?-lactoglobulin genetic variants A, B and C using (1)H NMR and fluorescence quenching.
Biochim Biophys Acta. 2014 Feb 28;
Authors: Keppler JK, Sönnichsen FD, Lorenzen PC, Schwarz K
Abstract
The structure of...
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03-05-2014 11:57 PM
[NMR paper] STARD5 specific ligand binding: Comparison with STARD1 and STARD4 subfamilies.
STARD5 specific ligand binding: Comparison with STARD1 and STARD4 subfamilies.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles STARD5 specific ligand binding: Comparison with STARD1 and STARD4 subfamilies.
Mol Cell Endocrinol. 2013 Jan 19;
Authors: Létourneau D, Lefebvre A, Lavigne P, Lehoux JG
Abstract
We present herein a review of our recent results on the characterization of the binding sites of STARD1, STARD5 and STARD6 using NMR and other biophysical...
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02-03-2013 10:19 AM
[NMR paper] Comparison of protein backbone entropy and beta-sheet stability: NMR-derived dynamics
Comparison of protein backbone entropy and beta-sheet stability: NMR-derived dynamics of protein G B1 domain mutants.
Related Articles Comparison of protein backbone entropy and beta-sheet stability: NMR-derived dynamics of protein G B1 domain mutants.
J Am Chem Soc. 2001 Jan 10;123(1):185-6
Authors: Stone MJ, Gupta S, Snyder N, Regan L
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11-19-2010 08:32 PM
[NMR paper] Comparison of X-ray and NMR structures for the Antennapedia homeodomain-DNA complex.
Comparison of X-ray and NMR structures for the Antennapedia homeodomain-DNA complex.
Related Articles Comparison of X-ray and NMR structures for the Antennapedia homeodomain-DNA complex.
Nat Struct Biol. 1998 Aug;5(8):692-7
Authors: Fraenkel E, Pabo CO
Homeodomains are one of the key families of eukaryotic DNA-binding motifs and provide an important model system for studying protein-DNA interactions. We have crystallized the Antennapedia homeodomain-DNA complex and solved this structure at 2.4 A resolution. NMR and molecular dynamics studies...