recent advances in the analysis of macromolecular interactions using the matrix-free method of sedimentation in the analytical ultracentrifuge

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ID: 216255
2015
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Abstract
Sedimentation in the analytical ultracentrifuge is a matrix free solution technique with no immobilisation, columns, or membranes required and can be used to study self-association and complex or “hetero”-interactions, stoichiometry, reversibility and interaction strength of a wide variety of macromolecular types and across a very large dynamic range (dissociation constants from 10−12 M to 10−1 M). We extend an earlier review specifically highlighting advances in sedimentation velocity and sedimentation equilibrium in the analytical ultracentrifuge applied to protein interactions and mucoadhesion and to review recent applications in protein self-association (tetanus toxoid, agrin), protein-like carbohydrate association (aminocelluloses), carbohydrate-protein interactions (polysaccharide-gliadin), nucleic-acid protein (G-duplexes), nucleic acid-carbohydrate (DNA-chitosan) and finally carbohydrate-carbohydrate (xanthan-chitosan and a ternary polysaccharide complex) interactions.
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harding2015biologyrecent Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors ;Stephen E. Harding;Richard B. Gillis;Fahad Almutairi;Tayyibe Erten;M. Şamil Kök;Gary G. Adams
Journal Journal of microencapsulation
Year 2015
DOI
10.3390/biology4010237
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