[NMR paper] Carbohydrate-polypeptide contacts in the antibody receptor CD16A identified through solution NMR spectroscopy.
Carbohydrate-polypeptide contacts in the antibody receptor CD16A identified through solution NMR spectroscopy.
Carbohydrate-polypeptide contacts in the antibody receptor CD16A identified through solution NMR spectroscopy.
Biochemistry. 2017 Jun 14;:
Authors: Subedi GP, Falconer DJ, Barb AW
Abstract
Asparagine-linked carbohydrates (N-glycans) are a common modification of eukaryotic proteins that confer multiple properties including the essential stabilization of therapeutic monoclonal antibodies. Here we present a rapid and...
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06-15-2017 03:37 PM
[NMR paper] Characterization of Protein-Carbohydrate Interactions by NMR Spectroscopy.
Characterization of Protein-Carbohydrate Interactions by NMR Spectroscopy.
Related Articles Characterization of Protein-Carbohydrate Interactions by NMR Spectroscopy.
Methods Mol Biol. 2017;1588:143-156
Authors: Grondin JM, Langelaan DN, Smith SP
Abstract
Solution-state nuclear magnetic resonance (NMR) spectroscopy can be used to monitor protein-carbohydrate interactions. Two-dimensional (1)H-(15)N heteronuclear single quantum coherence (HSQC)-based techniques described in this chapter can be used quickly and effectively to...
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04-19-2017 01:07 PM
[NMR paper] NMR analysis of carbohydrate-binding interactions in solution: an approach using analysis of saturation transfer difference NMR spectroscopy.
NMR analysis of carbohydrate-binding interactions in solution: an approach using analysis of saturation transfer difference NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR analysis of carbohydrate-binding interactions in solution: an approach using analysis of saturation transfer difference NMR spectroscopy.
Methods Mol Biol. 2014;1200:501-9
Authors: Hemmi H
Abstract
One of the most commonly used...
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04-09-2015 03:47 AM
[NMR paper] Solution NMR analyses of the C-type carbohydrate recognition domain of DC-SIGNR reveal different binding modes for HIV-derived oligosaccharides and smaller glycan fragments.
Solution NMR analyses of the C-type carbohydrate recognition domain of DC-SIGNR reveal different binding modes for HIV-derived oligosaccharides and smaller glycan fragments.
Related Articles Solution NMR analyses of the C-type carbohydrate recognition domain of DC-SIGNR reveal different binding modes for HIV-derived oligosaccharides and smaller glycan fragments.
J Biol Chem. 2013 Jun 20;
Authors: Probert F, Whittaker SB, Crispin M, Mitchell DA, Dixon AM
Abstract
The C-type lectin DC-SIGNR (Dendritic Cell-Specific ICAM-3-Grabbing...
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06-25-2013 12:17 AM
Probing water-protein contacts in a MMP-12/CGS27023A complex by nuclear magnetic resonance spectroscopy
Probing water-protein contacts in a MMP-12/CGS27023A complex by nuclear magnetic resonance spectroscopy
Abstract Using the case of the catalytic domain of MMP-12 in complex with the known inhibitor CGS27023A, a recently assembled 3D 15N-edited/14N,12C-filtered ROESY experiment is used to monitor and distinguish protein amide protons in fast exchange with bulk water from amide protons close to water molecules with longer residence times, the latter possibly reflecting water molecules of structural or functional importance. The 15N-edited/14N,12C-filtered ROESY spectra were compared to...
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04-19-2012 06:45 AM
Interactions between CusF and CusB Identified by NMR Spectroscopy and Chemical Cross-Linking Coupled to Mass Spectrometry
Interactions between CusF and CusB Identified by NMR Spectroscopy and Chemical Cross-Linking Coupled to Mass Spectrometry
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi102012j/aop/images/medium/bi-2010-02012j_0006.gif
Biochemistry
DOI: 10.1021/bi102012j
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03-09-2011 04:19 AM
Interactions between CusF and CusB identified by NMR spectroscopy and chemical cross-linking coupled to mass spectrometry.
Interactions between CusF and CusB identified by NMR spectroscopy and chemical cross-linking coupled to mass spectrometry.
Interactions between CusF and CusB identified by NMR spectroscopy and chemical cross-linking coupled to mass spectrometry.
Biochemistry. 2011 Feb 16;
Authors: Mealman TD, Bagai I, Singh P, Goodlet DR, Rensing C, Zhou H, Wysocki VH, McEvoy MM
The E. coli periplasmic proteins CusF and CusB, as part of the CusCFBA efflux system, aid in the resistance of elevated levels of copper and silver by direct metal transfer between the...
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02-18-2011 08:07 PM
[NMR paper] Transient hydrogen bonds identified on the surface of the NMR solution structure of H
Transient hydrogen bonds identified on the surface of the NMR solution structure of Hirudin.
Related Articles Transient hydrogen bonds identified on the surface of the NMR solution structure of Hirudin.
Biochemistry. 1994 Aug 9;33(31):9303-10
Authors: Szyperski T, Antuch W, Schick M, Betz A, Stone SR, Wüthrich K
Recombinant desulfatohirudin retains largely the thrombin-inhibitory activity of natural hirudin from Hirudo medicinalis and causes at most minimal immune response in humans. With regard to potential pharmaceutical applications it is...
Carbohydrate–Polypeptide Contacts in the AntibodyReceptor CD16A Identified through Solution NMR Spectroscopy
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