Related ArticlesThe Use of NMR to Study Transient Carbohydrate-Protein Interactions.
Front Mol Biosci. 2018;5:33
Authors: Nieto PM
Abstract
Carbohydrates are biologically ubiquitous and are essential to the existence of all known living organisms. Although they are better known for their role as energy sources (glucose/glycogen or starch) or structural elements (chitin or cellulose), carbohydrates also participate in the recognition events of molecular recognition processes. Such interactions with other biomolecules (nucleic acids, proteins, and lipids) are fundamental to life and disease. This review focuses on the application of NMR methods to understand at the atomic level the mechanisms by which sugar molecules can be recognized by proteins to form complexes, creating new entities with different properties to those of the individual component molecules. These processes have recently gained attention as new techniques have been developed, while at the same time old techniques have been reinvented and adapted to address newer emerging problems.
[NMR paper] Applications of NMR and ITC for the Study of the Kinetics of Carbohydrate Binding by AMPK ?-Subunit Carbohydrate-Binding Modules.
Applications of NMR and ITC for the Study of the Kinetics of Carbohydrate Binding by AMPK ?-Subunit Carbohydrate-Binding Modules.
Applications of NMR and ITC for the Study of the Kinetics of Carbohydrate Binding by AMPK ?-Subunit Carbohydrate-Binding Modules.
Methods Mol Biol. 2018;1732:87-98
Authors: Gooley PR, Koay A, Mobbs JI
Abstract
Understanding the kinetics of proteins interacting with their ligands is important for characterizing molecular mechanism. However, it can be difficult to determine the extent and nature of...
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[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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[NMR paper] The study of transient protein-nanoparticle interactions by solution NMR spectroscopy.
The study of transient protein-nanoparticle interactions by solution NMR spectroscopy.
Related Articles The study of transient protein-nanoparticle interactions by solution NMR spectroscopy.
Biochim Biophys Acta. 2015 Apr 30;
Authors: Assfalg M, Ragona L, Pagano K, D'Onofrio M, Zanzoni S, Tomaselli S, Molinari H
Abstract
The rapid development of novel nanoscale materials for applications in biomedicine urges an improved characterization of the nano-bio interfaces. Nanoparticles exhibit unique structures and properties, often...
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The study of transient protein-nanoparticle interactions by solution NMR spectroscopy
The study of transient protein-nanoparticle interactions by solution NMR spectroscopy
Publication date: Available online 30 April 2015
Source:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics</br>
Author(s): Michael Assfalg , Laura Ragona , Katiuscia Pagano , Mariapina D’Onofrio , Serena Zanzoni , Simona Tomaselli , Henriette Molinari</br>
The rapid development of novel nanoscale materials for applications in biomedicine urges an improved characterization of the nano-bio interfaces. Nanoparticles exhibit unique structures and properties, often...
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04-30-2015 09:13 PM
[NMR paper] Transient electrostatic interactions dominate the conformational equilibrium sampled by multi-domain splicing factor U2AF65: A combined NMR and SAXS study.
Transient electrostatic interactions dominate the conformational equilibrium sampled by multi-domain splicing factor U2AF65: A combined NMR and SAXS study.
Related Articles Transient electrostatic interactions dominate the conformational equilibrium sampled by multi-domain splicing factor U2AF65: A combined NMR and SAXS study.
J Am Chem Soc. 2014 Apr 16;
Authors: Huang JR, Warner LR, Sanchez C, Gabel F, Madl T, Mackereth CD, Sattler M, Blackledge M
Abstract
Multi-domain proteins containing intrinsically disordered linkers exhibit...
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04-17-2014 12:03 PM
[NMR paper] Characterizing carbohydrate-protein interactions by NMR.
Characterizing carbohydrate-protein interactions by NMR.
Characterizing carbohydrate-protein interactions by NMR.
Biopolymers. 2013 Jun 20;
Authors: Bewley CA, Shahzad-Ul-Hussan S
Abstract
Interactions between proteins and soluble carbohydrates and/or surface displayed glycans are central to countless recognition, attachment and signaling events in biology. The physical chemical features associated with these binding events vary considerably, depending on the biological system of interest. For example, carbohydrate-protein...
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06-21-2013 01:10 PM
Carbohydrate-Protein Interactions: A 3D View by NMR.
Carbohydrate-Protein Interactions: A 3D View by NMR.
Carbohydrate-Protein Interactions: A 3D View by NMR.
Chembiochem. 2011 Apr 15;
Authors: Roldós V, Cañada FJ, Jiménez-Barbero J
This review focuses on the application of NMR methods for understanding, at the molecular and atomic levels, the diverse mechanisms by which sugar molecules are recognised by the binding sites of lectins, antibodies and enzymes. Given the intrinsic chemical natures of sugars and their flexibility, it is well established that NMR parameters should be complemented by...
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04-19-2011 11:01 PM
[NMR paper] New structural insights into carbohydrate-protein interactions from NMR spectroscopy.
New structural insights into carbohydrate-protein interactions from NMR spectroscopy.
Related Articles New structural insights into carbohydrate-protein interactions from NMR spectroscopy.
Curr Opin Struct Biol. 2003 Oct;13(5):646-53
Authors: Kogelberg H, Solís D, Jiménez-Barbero J
Recently developed NMR methods have been applied to discover carbohydrate ligands for proteins and to identify their binding epitopes. The structural details of carbohydrate-protein complexes have also been examined by NMR, providing site-specific information on the...
The Use of NMR to Study Transient Carbohydrate-Protein Interactions.
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