Title : Study on the interactions between ginsenosides and lysozyme under acidic condition by ESI-MS and molecular docking.

Pub. Date : 2011 Feb

PMID : 21183401






6 Functional Relationships(s)
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1 Study on the interactions between ginsenosides and lysozyme under acidic condition by ESI-MS and molecular docking. Ginsenosides lysozyme Homo sapiens
2 The 1:1 and 2:1 noncovalent complexes of ginsenosides and lysozyme were observed in the mass spectra and the dissociation constants for them were directly calculated based on peak intensities of lysozyme and its noncovalent complexes with ginsenosides. Ginsenosides lysozyme Homo sapiens
3 The 1:1 and 2:1 noncovalent complexes of ginsenosides and lysozyme were observed in the mass spectra and the dissociation constants for them were directly calculated based on peak intensities of lysozyme and its noncovalent complexes with ginsenosides. Ginsenosides lysozyme Homo sapiens
4 The results showed that the 1:1 complex of ginsenoside Rg1 and lysozyme was more stable than that of ginsenoside Re and lysozyme. Ginsenosides lysozyme Homo sapiens
5 The results showed that the 1:1 complex of ginsenoside Rg1 and lysozyme was more stable than that of ginsenoside Re and lysozyme. Ginsenosides lysozyme Homo sapiens
6 From the result of molecular docking, ginsenosides interacted with the active sites of lysozyme. Ginsenosides lysozyme Homo sapiens