Publication date: 2 February 2018 Source:Biophysical Journal, Volume 114, Issue 3, Supplement 1
Author(s): Anton V. Sinitskiy, Ganesh P. Subedi, Adam W. Barb, Vijay S. Pande
[NMR paper] Protein-Glycan Quinary Interactions in Crowding Environment Unveiled by NMR Spectroscopy.
Protein-Glycan Quinary Interactions in Crowding Environment Unveiled by NMR Spectroscopy.
Related Articles Protein-Glycan Quinary Interactions in Crowding Environment Unveiled by NMR Spectroscopy.
Chemistry. 2017 Jun 25;:
Authors: Diniz A, S Dias J, Jiménez-Barbero J, Marcelo F, Cabrita EJ
Abstract
Protein-glycan interactions as modulators for quinary structure in crowding environments were explored. The interaction between human galectin 3 (Gal-3) and distinct macromolecular crowders, such as bovine and human serum albumin (BSA...
Neisserial Opa Protein–CEACAM Interactions:Competition for Receptors as a Means of Bacterial Invasion and Pathogenesis
Neisserial Opa Protein–CEACAM Interactions:Competition for Receptors as a Means of Bacterial Invasion and Pathogenesis
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00124/20160729/images/medium/bi-2016-00124x_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00124
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
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08-01-2016 10:34 PM
[NMR paper] Monitoring Glycan-Protein Interactions by NMR Spectroscopic Analysis: A Simple Chemical Tag That Mimics Natural CH-? Interactions.
Monitoring Glycan-Protein Interactions by NMR Spectroscopic Analysis: A Simple Chemical Tag That Mimics Natural CH-? Interactions.
Related Articles Monitoring Glycan-Protein Interactions by NMR Spectroscopic Analysis: A Simple Chemical Tag That Mimics Natural CH-? Interactions.
Chemistry. 2015 Jul 14;
Authors: Calle LP, Echeverria B, Franconetti A, Serna S, Fernández-Alonso MC, Diercks T, Cañada FJ, Ardá A, Reichardt NC, Jiménez-Barbero J
Abstract
Detection of molecular recognition processes requires robust, specific, and easily...
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07-17-2015 03:02 PM
[NMR paper] Fluorinated Carbohydrates as Lectin Ligands: Dissecting Glycan-Cyanovirin Interactions by Using 19 F NMR Spectroscopy.
Fluorinated Carbohydrates as Lectin Ligands: Dissecting Glycan-Cyanovirin Interactions by Using 19 F NMR Spectroscopy.
Fluorinated Carbohydrates as Lectin Ligands: Dissecting Glycan-Cyanovirin Interactions by Using 19 F NMR Spectroscopy.
Chemistry. 2013 Feb 28;
Authors: Matei E, André S, Glinschert A, Infantino AS, Oscarson S, Gabius HJ, Gronenborn AM
Abstract
NMR spectroscopy and isothermal titration calorimetry (ITC) are powerful methods to investigate ligand-protein interactions. Here, we present a versatile and sensitive fluorine NMR...
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03-01-2013 09:57 PM
Protein structure modeling using sparse NMR data [Biophysics and Computational Biology]
Protein structure modeling using sparse NMR data
Thompson, J. M., Sgourakis, N. G., Liu, G., Rossi, P., Tang, Y., Mills, J. L., Szyperski, T., Montelione, G. T., Baker, D....
Date: 2012-06-19
While information from homologous structures plays a central role in X-ray structure determination by molecular replacement, such information is rarely used in NMR structure determination because it can be incorrect, both locally and globally, when evolutionary relationships are inferred incorrectly or there has been considerable evolutionary structural divergence. Here we describe a method that...
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06-20-2012 02:28 AM
Opioid receptors revealed - Nature.com
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Opioid receptors revealed
Nature.com
Kobilka, Stevens and many others are complementing crystallography with techniques that can capture protein movement, such as nuclear magnetic resonance and molecular-dynamics modelling. On Stevens's website, where the tree of dreams is prominently ...
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Opioid receptors revealed - Nature.com
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03-21-2012 11:40 PM
Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy [Biophysics and Computational Biology]
Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy
Masterson, L. R., Shi, L., Metcalfe, E., Gao, J., Taylor, S. S., Veglia, G....
Date: 2011-04-26
Protein kinase A (PKA) is a ubiquitous phosphoryl transferase that mediates hundreds of cell signaling events. During turnover, its catalytic subunit (PKA-C) interconverts between three major conformational states (open, intermediate, and closed) that are dynamically and allosterically activated by nucleotide binding. We show that the structural transitions between these...
Glycan-Protein Interactions in NMDA Receptors Revealed with Computational Modeling and NMR Spectroscopy
Linear Mode
