Related Articles(19)F labelled glycosaminoglycan probes for solution NMR and non-linear (CARS) microscopy.
Glycoconj J. 2016 Aug 15;
Authors: Lima MA, Cavalheiro RP, M Viana G, Meneghetti MC, Rudd TR, Skidmore MA, Powell AK, Yates EA
Abstract
Studying polysaccharide-protein interactions under physiological conditions by conventional techniques is challenging. Ideally, macromolecules could be followed by both in vitro spectroscopy experiments as well as in tissues using microscopy, to enable a proper comparison of results over these different scales but, often, this is not feasible. The cell surface and extracellular matrix polysaccharides, glycosaminoglycans (GAGs) lack groups that can be detected selectively in the biological milieu. The introduction of (19)F labels into GAG polysaccharides is explored and the interaction of a labelled GAG with the heparin-binding protein, antithrombin, employing (19)F NMR spectroscopy is followed. Furthermore, the ability of (19)F labelled GAGs to be imaged using CARS microscopy is demonstrated. (19)F labelled GAGs enable both (19)F NMR protein-GAG binding studies in solution at the molecular level and non-linear microscopy at a microscopic scale to be conducted on the same material, essentially free of background signals.
PMID: 27523650 [PubMed - as supplied by publisher]
[NMR paper] NMR insight into the multiple glycosaminoglycan binding modes of the Link module from human TSG-6.
NMR insight into the multiple glycosaminoglycan binding modes of the Link module from human TSG-6.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles NMR insight into the multiple glycosaminoglycan binding modes of the Link module from human TSG-6.
Biochemistry. 2015 Dec 18;
Authors: Park Y, Jowitt TA, Day AJ, Prestegard JH
Abstract
Tumor necrosis factor-stimulated gene-6 (TSG-6) is a hyaluronan (HA) binding protein that is essential for stabilizing and...
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[NMR paper] Identification of the Glycosaminoglycan Binding Site of Interleukin-10 by NMR Spectroscopy.
Identification of the Glycosaminoglycan Binding Site of Interleukin-10 by NMR Spectroscopy.
Related Articles Identification of the Glycosaminoglycan Binding Site of Interleukin-10 by NMR Spectroscopy.
J Biol Chem. 2015 Dec 16;
Authors: Künze G, Köhling S, Vogel A, Rademann J, Huster D
Abstract
The biological function of interleukin-10 (IL-10), a pleiotropic cytokine with an essential role in inflammatory processes, is known to be affected by glycosaminoglycans (GAGs). GAGs are highly negatively charged polysaccharides and...
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Fluorescence Microscopy and Solution NMR Studies of Cytoskeletal Proteins from Tetrahymena
Fluorescence Microscopy and Solution NMR Studies of Cytoskeletal Proteins from Tetrahymena
Publication date: 27 January 2015
Source:Biophysical Journal, Volume 108, Issue 2, Supplement 1</br>
Author(s): Robert Sterner , Jerry Honts , Adina Kilpatrick</br>
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[NMR paper] Characterizing protein-glycosaminoglycan interactions using solution NMR spectroscopy.
Characterizing protein-glycosaminoglycan interactions using solution NMR spectroscopy.
Characterizing protein-glycosaminoglycan interactions using solution NMR spectroscopy.
Methods Mol Biol. 2015;1229:325-33
Authors: Joseph PR, Poluri KM, Sepuru KM, Rajarathnam K
Abstract
Solution nuclear magnetic resonance (NMR) spectroscopy and, in particular, chemical shift perturbation (CSP) titration experiments are ideally suited for characterizing the binding interface of macromolecular complexes. (1)H-(15) N-HSQC-based CSP studies have...
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[NMR paper] Characterization of the spherical intermediates and fibril formation of hCT in HEPES solution using solid-state 13C-NMR and transmission electron microscopy.
Characterization of the spherical intermediates and fibril formation of hCT in HEPES solution using solid-state 13C-NMR and transmission electron microscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Related Articles Characterization of the spherical intermediates and fibril formation of hCT in HEPES solution using solid-state 13C-NMR and transmission electron microscopy.
Phys Chem Chem Phys. 2013 Oct 21;15(39):16956-64
Authors: Itoh-Watanabe H, Kamihira-Ishijima M,...
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[NMR paper] Solution NMR Studies on the Orientation of Membrane-Bound Peptides and Proteins by Paramagnetic Probes.
Solution NMR Studies on the Orientation of Membrane-Bound Peptides and Proteins by Paramagnetic Probes.
Solution NMR Studies on the Orientation of Membrane-Bound Peptides and Proteins by Paramagnetic Probes.
Molecules. 2013;18(7):7407-7435
Authors: Schrank E, Wagner GE, Zangger K
Abstract
Many peptides and proteins are attached to or immersed in a biological membrane. In order to understand their function not only the structure but also their topology in the membrane is important. Solution NMR spectroscopy is one of the most often...
[NMR paper] Identification of a novel glycosaminoglycan core-like molecule. I. 500 MHz 1H NMR ana
Identification of a novel glycosaminoglycan core-like molecule. I. 500 MHz 1H NMR analysis using a nano-NMR probe indicates the presence of a terminal alpha-GalNAc residue capping 4-methylumbelliferyl-beta-D-xylosides.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles Identification of a novel glycosaminoglycan core-like molecule. I. 500 MHz 1H NMR analysis using a nano-NMR probe indicates the presence of a terminal alpha-GalNAc residue capping...