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NMR studies on the conformation of polyflavanoids and their association with proteinsAuthor(s): Richard W. Hemingway; Petrus J. Steynberg; Jan P. Steynberg; Tsutomu. Hatano
Source: In: Argyropoulos, Dimitris S., ed.Advances inlignocellulosics characterization.Atlanta, GA:TAPPI Press:157-178.
Publication Series: Miscellaneous Publication
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DescriptionPolyflavanoids (also named condensed tannins or proanthocyanidins) make up approximately half of the dry weight of most commercial tree barks, are often found in even higher concentrations in nut shells, and are important constituents of the leaves of plants. The polyflavanoids rank second in abundance after lignin as a source of renewable phenolic materials. Most of their commercial and ecological significance centers on either their propensity to form complexes with proteins or on their potent antioxidant propertiesBecause it is believed that the association of polyflavanoids with proteins is dictated by the shape and flexibility of these molecules, the authors have undertaken an effort to try to define the conformational dynamics of polyflavanoids and to learn more about the interaction of polyflavanoids with proteins. The authors’ approach has been centered mainly on NMR experiments to obtain the necessary physical data to evaluate the results of computational chemistry. Both NMR instrumentation and computational chemistry software are advancing at a fast pace and increasingly offer avenues to solution of questions surrounding tannin/protein interactions
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CitationHemingway, Richard W.; Steynberg, Petrus J.; Steynberg, Jan P.; Hatano, Tsutomu. 1999. NMR studies on the conformation of polyflavanoids and their association with proteins. In: Argyropoulos, Dimitris S., ed.Advances inlignocellulosics characterization.Atlanta, GA:TAPPI Press:157-178.
- Exploring the conformations of polyflavanoids – an approach to understanding the significance of tannins
- Conformational dynamics of proanthocyanidins: physical and computational approaches
- Modeling the conformation of polyphenols and their complexation with polypeptides: self-association of catechin and its complexation with L-proline glycine oligomers.
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